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P02879

- RICI_RICCO

UniProt

P02879 - RICI_RICCO

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Protein

Ricin

Gene
N/A
Organism
Ricinus communis (Castor bean)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

GO - Biological processi

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

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
Complete GO annotation...

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. 1 Publication
Mutagenesisi109 – 1091L → A or M: No effect on the toxic activity or the vascular leak syndrome. 1 Publication
Mutagenesisi110 – 1101D → A, E or N: Suppresses the toxic activity. 1 Publication
Mutagenesisi111 – 1111V → A or M: No effect on the toxic activity or the vascular leak syndrome. 1 Publication
Mutagenesisi132 – 1321N → A: No effect on the toxic activity but Suppresses the vascular leak syndrome. 1 Publication

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MKPGGNTIVI WMYAVATWLC FGSTSGWSFT LEDNNIFPKQ YPIINFTTAG
60 70 80 90 100
ATVQSYTNFI RAVRGRLTTG ADVRHEIPVL PNRVGLPINQ RFILVELSNH
110 120 130 140 150
AELSVTLALD VTNAYVVGYR AGNSAYFFHP DNQEDAEAIT HLFTDVQNRY
160 170 180 190 200
TFAFGGNYDR LEQLAGNLRE NIELGNGPLE EAISALYYYS TGGTQLPTLA
210 220 230 240 250
RSFIICIQMI SEAARFQYIE GEMRTRIRYN RRSAPDPSVI TLENSWGRLS
260 270 280 290 300
TAIQESNQGA FASPIQLQRR NGSKFSVYDV SILIPIIALM VYRCAPPPSS
310 320 330 340 350
QFSLLIRPVV PNFNADVCMD PEPIVRIVGR NGLCVDVRDG RFHNGNAIQL
360 370 380 390 400
WPCKSNTDAN QLWTLKRDNT IRSNGKCLTT YGYSPGVYVM IYDCNTAATD
410 420 430 440 450
ATRWQIWDNG TIINPRSSLV LAATSGNSGT TLTVQTNIYA VSQGWLPTNN
460 470 480 490 500
TQPFVTTIVG LYGLCLQANS GQVWIEDCSS EKAEQQWALY ADGSIRPQQN
510 520 530 540 550
RDNCLTSDSN IRETVVKILS CGPASSGQRW MFKNDGTILN LYSGLVLDVR
560 570
ASDPSLKQII LYPLHGDPNQ IWLPLF
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.Curated
The sequence described in 1 Publication differs from that shown. Reason: High number of conflicts with the sequence translated from DNA.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.

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: November 26, 2014
This is version 151 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

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