Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P02879

- RICI_RICCO

UniProt

P02879 - RICI_RICCO

Protein

Ricin

Gene
N/A
Organism
Ricinus communis (Castor bean)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Ricin is highly toxic to animal cells and to a lesser extent to plant cells. The A chain acts as a glycosidase that removes a specific adenine residue from an exposed loop of the 28S rRNA (A4324 in mammals), leading to rRNA breakage. As this loop is involved in elongation factor binding, modified ribosomes are catalytically inactive and unable to support protein synthesis. The A chain can inactivate a few thousand ribosomes per minute, faster than the cell can make new ones. Therefore a single A chain molecule can kill an animal cell. The B chain binds to beta-D-galactopyranoside moieties on cell surface glycoproteins and glycolipids and facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (Lectin activity).

    Catalytic activityi

    Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei50 – 501Carbohydrate; via amide nitrogen
    Binding sitei85 – 851Carbohydrate; via amide nitrogen
    Active sitei212 – 2121
    Binding sitei324 – 3241Carbohydrate; via carbonyl oxygenBy similarity
    Binding sitei349 – 3491Carbohydrate
    Binding sitei354 – 3541Carbohydrate
    Binding sitei360 – 3601Carbohydrate
    Binding sitei409 – 4091CarbohydrateBy similarity
    Binding sitei449 – 4491CarbohydrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi115 – 1162AMP
    Nucleotide bindingi156 – 1583AMP

    GO - Molecular functioni

    1. nucleotide binding Source: UniProtKB-KW
    2. rRNA N-glycosylase activity Source: UniProtKB-EC

    GO - Biological processi

    1. defense response Source: UniProtKB-KW
    2. negative regulation of translation Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protein synthesis inhibitor, Toxin

    Keywords - Biological processi

    Plant defense

    Keywords - Ligandi

    Lectin, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi3.2.2.22. 1204.

    Protein family/group databases

    CAZyiCBM13. Carbohydrate-Binding Module Family 13.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ricin
    Cleaved into the following 3 chains:
    Alternative name(s):
    rRNA N-glycosidase
    OrganismiRicinus communis (Castor bean)
    Taxonomic identifieri3988 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeAcalyphoideaeAcalypheaeRicinus

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB

    Pathology & Biotechi

    Biotechnological usei

    A deglycosylated A chain may be linked to monoclonal antibodies to produce immunotoxins exploited in cancer treatment. However, a point mutation should be introduced to eliminate vascular leak syndrome, a side effect resulting from endothelial damage.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi83 – 831R → A: No effect on the toxic activity but suppresses the vascular leak syndrome. 2 Publications
    Mutagenesisi109 – 1091L → A or M: No effect on the toxic activity or the vascular leak syndrome. 2 Publications
    Mutagenesisi110 – 1101D → A, E or N: Suppresses the toxic activity. 2 Publications
    Mutagenesisi111 – 1111V → A or M: No effect on the toxic activity or the vascular leak syndrome. 2 Publications
    Mutagenesisi132 – 1321N → A: No effect on the toxic activity but Suppresses the vascular leak syndrome. 2 Publications

    Protein family/group databases

    Allergomei2803. Ric c RIP.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 35351 PublicationAdd
    BLAST
    Chaini36 – 302267Ricin A chainPRO_0000030741Add
    BLAST
    Peptidei303 – 31412Linker peptide1 PublicationPRO_0000030742Add
    BLAST
    Chaini315 – 576262Ricin B chainPRO_0000030743Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi45 – 451N-linked (GlcNAc...)1 PublicationCAR_000080
    Glycosylationi271 – 2711N-linked (GlcNAc...); partial1 PublicationCAR_000081
    Disulfide bondi294 ↔ 318Interchain (between A and B chains)
    Disulfide bondi334 ↔ 353
    Disulfide bondi377 ↔ 394
    Glycosylationi409 – 4091N-linked (GlcNAc...)
    Glycosylationi449 – 4491N-linked (GlcNAc...)
    Disulfide bondi465 ↔ 478
    Disulfide bondi504 ↔ 521

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    PTM databases

    UniCarbKBiP02879.

    Interactioni

    Subunit structurei

    Disulfide-linked dimer of A and B chains.

    Protein-protein interaction databases

    BioGridi1022023. 1 interaction.
    DIPiDIP-46421N.
    IntActiP02879. 2 interactions.
    MINTiMINT-8391414.

    Structurei

    Secondary structure

    1
    576
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi43 – 486
    Helixi53 – 6715
    Beta strandi72 – 743
    Beta strandi77 – 793
    Turni83 – 853
    Helixi88 – 903
    Beta strandi91 – 988
    Beta strandi100 – 1023
    Beta strandi104 – 1107
    Turni111 – 1133
    Beta strandi116 – 1216
    Beta strandi124 – 1274
    Helixi133 – 1397
    Turni140 – 1456
    Beta strandi147 – 1515
    Helixi158 – 1658
    Turni166 – 1683
    Helixi169 – 1713
    Helixi176 – 18813
    Helixi189 – 1913
    Helixi196 – 21520
    Helixi217 – 22812
    Helixi237 – 25418
    Beta strandi260 – 2689
    Beta strandi270 – 2723
    Beta strandi274 – 2796
    Helixi280 – 2834
    Turni284 – 2863
    Beta strandi298 – 3003
    Helixi330 – 3323
    Beta strandi334 – 3374
    Helixi338 – 3403
    Beta strandi347 – 3515
    Helixi359 – 3613
    Beta strandi363 – 3653
    Beta strandi369 – 3735
    Beta strandi376 – 3816
    Beta strandi388 – 3936
    Turni394 – 3963
    Helixi399 – 4013
    Beta strandi412 – 4143
    Turni415 – 4184
    Beta strandi419 – 4224
    Beta strandi433 – 4364
    Helixi441 – 4433
    Beta strandi454 – 4596
    Helixi461 – 4633
    Beta strandi465 – 4695
    Beta strandi472 – 4765
    Turni480 – 4834
    Beta strandi487 – 4893
    Beta strandi495 – 4973
    Beta strandi503 – 5075
    Beta strandi516 – 5216
    Helixi526 – 5283
    Turni541 – 5433
    Beta strandi546 – 5494
    Helixi550 – 5523
    Helixi554 – 5563
    Beta strandi559 – 5624
    Helixi568 – 5703
    Beta strandi573 – 5753

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BR5X-ray2.50A36-302[»]
    1BR6X-ray2.30A36-302[»]
    1IFSX-ray2.00A38-298[»]
    1IFTX-ray1.80A38-298[»]
    1IFUX-ray2.40A38-298[»]
    1IL3X-ray2.80A36-302[»]
    1IL4X-ray2.60A36-302[»]
    1IL5X-ray2.80A/B36-302[»]
    1IL9X-ray3.10A36-302[»]
    1J1MX-ray1.50A36-302[»]
    1OBSX-ray2.20A36-302[»]
    1OBTX-ray2.80A36-302[»]
    1RTCX-ray2.30A36-302[»]
    1UQ4X-ray1.90A40-302[»]
    1UQ5X-ray1.40A40-302[»]
    2AAIX-ray2.50A36-302[»]
    B315-576[»]
    2P8NX-ray1.94A36-302[»]
    2PJOX-ray1.80A36-302[»]
    2R2XX-ray2.40A36-302[»]
    2R3DX-ray2.09A36-302[»]
    2VC3X-ray1.60A36-302[»]
    2VC4X-ray1.39A36-302[»]
    3BJGX-ray2.14A36-302[»]
    3EJ5X-ray2.50X40-296[»]
    3HIOX-ray2.00A36-302[»]
    3LC9X-ray2.28A36-233[»]
    3MK9X-ray2.08A36-233[»]
    3PX8X-ray1.29X39-296[»]
    3PX9X-ray1.89X39-296[»]
    3RTIX-ray2.80A36-302[»]
    B315-576[»]
    3RTJX-ray3.00A36-302[»]
    B315-576[»]
    3SRPX-ray2.14A36-302[»]
    4ESIX-ray1.87A36-302[»]
    4HUOX-ray1.52X36-302[»]
    4HUPX-ray1.70X36-302[»]
    4HV3X-ray1.54A36-302[»]
    4HV7X-ray1.87X36-302[»]
    4IMVX-ray2.25A36-233[»]
    4KUCX-ray2.79A/I36-302[»]
    4LGPX-ray2.40A/C36-296[»]
    4LGRX-ray1.65A40-294[»]
    4LGSX-ray2.70A39-301[»]
    4LHJX-ray1.80A39-297[»]
    4LHQX-ray2.30A/C39-298[»]
    4MX1X-ray1.59A36-302[»]
    4MX5X-ray1.52X36-302[»]
    ProteinModelPortaliP02879.
    SMRiP02879. Positions 36-302, 315-576.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02879.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini321 – 448128Ricin B-type lectin 1PROSITE-ProRule annotationAdd
    BLAST
    Repeati331 – 373431-alphaAdd
    BLAST
    Repeati374 – 414411-betaAdd
    BLAST
    Repeati417 – 449331-gammaAdd
    BLAST
    Domaini451 – 575125Ricin B-type lectin 2PROSITE-ProRule annotationAdd
    BLAST
    Repeati462 – 497362-alphaAdd
    BLAST
    Repeati501 – 540402-betaAdd
    BLAST
    Repeati543 – 570282-gammaAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni43 – 453Carbohydrate bindingBy similarity
    Regioni176 – 1816Carbohydrate binding
    Regioni230 – 2323Carbohydrate binding
    Regioni336 – 3405Carbohydrate binding
    Regioni548 – 5514Carbohydrate binding
    Regioni565 – 5695Carbohydrate binding

    Domaini

    The B chain is composed of two domains, each domain consists of 3 homologous subdomains (alpha, beta, gamma).

    Sequence similaritiesi

    In the N-terminal section; belongs to the ribosome-inactivating protein family. Type 2 RIP subfamily.Curated
    Contains 2 ricin B-type lectin domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Family and domain databases

    Gene3Di3.40.420.10. 1 hit.
    4.10.470.10. 1 hit.
    InterProiIPR001574. Ribosome_inactivat_prot.
    IPR017988. Ribosome_inactivat_prot_CS.
    IPR016138. Ribosome_inactivat_prot_sub1.
    IPR016139. Ribosome_inactivat_prot_sub2.
    IPR017989. Ribosome_inactivat_prot_subgr.
    IPR000772. Ricin_B_lectin.
    [Graphical view]
    PfamiPF00652. Ricin_B_lectin. 2 hits.
    PF00161. RIP. 1 hit.
    [Graphical view]
    PRINTSiPR00396. SHIGARICIN.
    SMARTiSM00458. RICIN. 2 hits.
    [Graphical view]
    SUPFAMiSSF50370. SSF50370. 2 hits.
    SSF56371. SSF56371. 1 hit.
    PROSITEiPS50231. RICIN_B_LECTIN. 2 hits.
    PS00275. SHIGA_RICIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P02879-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKPGGNTIVI WMYAVATWLC FGSTSGWSFT LEDNNIFPKQ YPIINFTTAG    50
    ATVQSYTNFI RAVRGRLTTG ADVRHEIPVL PNRVGLPINQ RFILVELSNH 100
    AELSVTLALD VTNAYVVGYR AGNSAYFFHP DNQEDAEAIT HLFTDVQNRY 150
    TFAFGGNYDR LEQLAGNLRE NIELGNGPLE EAISALYYYS TGGTQLPTLA 200
    RSFIICIQMI SEAARFQYIE GEMRTRIRYN RRSAPDPSVI TLENSWGRLS 250
    TAIQESNQGA FASPIQLQRR NGSKFSVYDV SILIPIIALM VYRCAPPPSS 300
    QFSLLIRPVV PNFNADVCMD PEPIVRIVGR NGLCVDVRDG RFHNGNAIQL 350
    WPCKSNTDAN QLWTLKRDNT IRSNGKCLTT YGYSPGVYVM IYDCNTAATD 400
    ATRWQIWDNG TIINPRSSLV LAATSGNSGT TLTVQTNIYA VSQGWLPTNN 450
    TQPFVTTIVG LYGLCLQANS GQVWIEDCSS EKAEQQWALY ADGSIRPQQN 500
    RDNCLTSDSN IRETVVKILS CGPASSGQRW MFKNDGTILN LYSGLVLDVR 550
    ASDPSLKQII LYPLHGDPNQ IWLPLF 576
    Length:576
    Mass (Da):64,091
    Last modified:August 13, 1987 - v1
    Checksum:iC14C4B77A8B5470D
    GO

    Sequence cautioni

    The sequence described in 1 Publication differs from that shown. Reason: High number of conflicts with the sequence translated from DNA.
    The sequence described in 1 Publication differs from that shown. Reason: High number of conflicts with the sequence translated from DNA.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti76 – 761E → D in CAA26230. (PubMed:3838723)Curated
    Sequence conflicti551 – 5511A → R in CAA26230. (PubMed:3838723)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03179 Genomic DNA. Translation: CAA26939.1.
    X52908 Genomic DNA. Translation: CAA37095.1.
    X02388 mRNA. Translation: CAA26230.1.
    PIRiA24041. RLCSD.
    RefSeqiXP_002534649.1. XM_002534603.1.

    Genome annotation databases

    GeneIDi8287993.
    KEGGircu:RCOM_2159910.

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    Baneful beans - Issue 31 of February 2003

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03179 Genomic DNA. Translation: CAA26939.1 .
    X52908 Genomic DNA. Translation: CAA37095.1 .
    X02388 mRNA. Translation: CAA26230.1 .
    PIRi A24041. RLCSD.
    RefSeqi XP_002534649.1. XM_002534603.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BR5 X-ray 2.50 A 36-302 [» ]
    1BR6 X-ray 2.30 A 36-302 [» ]
    1IFS X-ray 2.00 A 38-298 [» ]
    1IFT X-ray 1.80 A 38-298 [» ]
    1IFU X-ray 2.40 A 38-298 [» ]
    1IL3 X-ray 2.80 A 36-302 [» ]
    1IL4 X-ray 2.60 A 36-302 [» ]
    1IL5 X-ray 2.80 A/B 36-302 [» ]
    1IL9 X-ray 3.10 A 36-302 [» ]
    1J1M X-ray 1.50 A 36-302 [» ]
    1OBS X-ray 2.20 A 36-302 [» ]
    1OBT X-ray 2.80 A 36-302 [» ]
    1RTC X-ray 2.30 A 36-302 [» ]
    1UQ4 X-ray 1.90 A 40-302 [» ]
    1UQ5 X-ray 1.40 A 40-302 [» ]
    2AAI X-ray 2.50 A 36-302 [» ]
    B 315-576 [» ]
    2P8N X-ray 1.94 A 36-302 [» ]
    2PJO X-ray 1.80 A 36-302 [» ]
    2R2X X-ray 2.40 A 36-302 [» ]
    2R3D X-ray 2.09 A 36-302 [» ]
    2VC3 X-ray 1.60 A 36-302 [» ]
    2VC4 X-ray 1.39 A 36-302 [» ]
    3BJG X-ray 2.14 A 36-302 [» ]
    3EJ5 X-ray 2.50 X 40-296 [» ]
    3HIO X-ray 2.00 A 36-302 [» ]
    3LC9 X-ray 2.28 A 36-233 [» ]
    3MK9 X-ray 2.08 A 36-233 [» ]
    3PX8 X-ray 1.29 X 39-296 [» ]
    3PX9 X-ray 1.89 X 39-296 [» ]
    3RTI X-ray 2.80 A 36-302 [» ]
    B 315-576 [» ]
    3RTJ X-ray 3.00 A 36-302 [» ]
    B 315-576 [» ]
    3SRP X-ray 2.14 A 36-302 [» ]
    4ESI X-ray 1.87 A 36-302 [» ]
    4HUO X-ray 1.52 X 36-302 [» ]
    4HUP X-ray 1.70 X 36-302 [» ]
    4HV3 X-ray 1.54 A 36-302 [» ]
    4HV7 X-ray 1.87 X 36-302 [» ]
    4IMV X-ray 2.25 A 36-233 [» ]
    4KUC X-ray 2.79 A/I 36-302 [» ]
    4LGP X-ray 2.40 A/C 36-296 [» ]
    4LGR X-ray 1.65 A 40-294 [» ]
    4LGS X-ray 2.70 A 39-301 [» ]
    4LHJ X-ray 1.80 A 39-297 [» ]
    4LHQ X-ray 2.30 A/C 39-298 [» ]
    4MX1 X-ray 1.59 A 36-302 [» ]
    4MX5 X-ray 1.52 X 36-302 [» ]
    ProteinModelPortali P02879.
    SMRi P02879. Positions 36-302, 315-576.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 1022023. 1 interaction.
    DIPi DIP-46421N.
    IntActi P02879. 2 interactions.
    MINTi MINT-8391414.

    Chemistry

    BindingDBi P02879.
    ChEMBLi CHEMBL4756.
    DrugBanki DB00173. Adenine.
    DB00131. Adenosine monophosphate.

    Protein family/group databases

    Allergomei 2803. Ric c RIP.
    CAZyi CBM13. Carbohydrate-Binding Module Family 13.

    PTM databases

    UniCarbKBi P02879.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 8287993.
    KEGGi rcu:RCOM_2159910.

    Enzyme and pathway databases

    BRENDAi 3.2.2.22. 1204.

    Miscellaneous databases

    EvolutionaryTracei P02879.

    Family and domain databases

    Gene3Di 3.40.420.10. 1 hit.
    4.10.470.10. 1 hit.
    InterProi IPR001574. Ribosome_inactivat_prot.
    IPR017988. Ribosome_inactivat_prot_CS.
    IPR016138. Ribosome_inactivat_prot_sub1.
    IPR016139. Ribosome_inactivat_prot_sub2.
    IPR017989. Ribosome_inactivat_prot_subgr.
    IPR000772. Ricin_B_lectin.
    [Graphical view ]
    Pfami PF00652. Ricin_B_lectin. 2 hits.
    PF00161. RIP. 1 hit.
    [Graphical view ]
    PRINTSi PR00396. SHIGARICIN.
    SMARTi SM00458. RICIN. 2 hits.
    [Graphical view ]
    SUPFAMi SSF50370. SSF50370. 2 hits.
    SSF56371. SSF56371. 1 hit.
    PROSITEi PS50231. RICIN_B_LECTIN. 2 hits.
    PS00275. SHIGA_RICIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genomic cloning and characterization of a ricin gene from Ricinus communis."
      Halling K.C., Halling A.C., Murray E.E., Ladin B.F., Houston L.L., Weaver R.F.
      Nucleic Acids Res. 13:8019-8033(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The lectin gene family of Ricinus communis: cloning of a functional ricin gene and three lectin pseudogenes."
      Tregear J.W., Roberts L.M.
      Plant Mol. Biol. 18:515-525(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Nucleotide sequence of cloned cDNA coding for preproricin."
      Lamb A., Roberts L.M., Lord J.M.
      Eur. J. Biochem. 148:265-270(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 12-576.
    4. "Isolation and sequences of peptic peptides, and the complete sequence of Ile chain of ricin-D."
      Yoshitake S., Funatsu G., Funatsu M.
      Agric. Biol. Chem. 42:1267-1274(1978)
      Cited for: PROTEIN SEQUENCE OF 36-302.
    5. "Primary structure of Ala chain of ricin D."
      Funatsu G., Kimura M., Funatsu M.
      Agric. Biol. Chem. 43:2221-2224(1979)
      [AGRICOLA] [Europe PMC]
      Cited for: PROTEIN SEQUENCE OF 315-576.
    6. "Structural analyses of sugar chains from ricin A-chain variant."
      Kimura Y., Kusuoku H., Tada M., Takagi S., Funatsu G.
      Agric. Biol. Chem. 54:157-162(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-45 AND ASN-271, PARTIAL PROTEIN SEQUENCE.
    7. Cited for: REVIEW.
    8. "The three-dimensional structure of ricin at 2.8 A."
      Monfort W., Villafranca J.E., Monzingo A.F., Ernst S.R., Katzin B., Rutenber E., Xuong N.H., Hamlin R., Robertus J.D.
      J. Biol. Chem. 262:5398-5403(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
    9. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF A-CHAIN.
    10. "Structure of ricin B-chain at 2.5-A resolution."
      Rutenber E., Robertus J.D.
      Proteins 10:260-269(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF B-CHAIN.
    11. "X-ray structure of recombinant ricin A-chain at 1.8-A resolution."
      Weston S.A., Tucker A.D., Thatcher D.R., Derbyshire D.J., Pauptit R.A.
      J. Mol. Biol. 244:410-422(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF A-CHAIN.
    12. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT HIS-215.
    13. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF A-CHAIN.
    14. "Analysis of several key active site residues of ricin A chain by mutagenesis and X-ray crystallography."
      Kin Y., Robertus J.D.
      Protein Eng. 5:775-779(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    15. "Genetic engineering of an immunotoxin to eliminate pulmonary vascular leak in mice."
      Smallshaw J.E., Ghetie V., Rizo J., Fulmer J.R., Trahan L.L., Ghetie M.-A., Vitetta E.S.
      Nat. Biotechnol. 21:387-391(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ARG-83; LEU-109; ASP-110; VAL-111 AND ASN-132.

    Entry informationi

    Entry nameiRICI_RICCO
    AccessioniPrimary (citable) accession number: P02879
    Secondary accession number(s): P02880
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 149 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3