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P81446

- ML1_VISAL

UniProt

P81446 - ML1_VISAL

Protein

Beta-galactoside-specific lectin 1

Gene
N/A
Organism
Viscum album (European mistletoe)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 3 (17 Apr 2007)
      Previous versions | rss
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    Functioni

    The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (lectin activity). Inhibits growth of the human tumor cell line Molt4.3 Publications

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei198 – 1981By similarity

    GO - Molecular functioni

    1. 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

    Protein family/group databases

    CAZyiCBM13. Carbohydrate-Binding Module Family 13.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-galactoside-specific lectin 1
    Alternative name(s):
    Beta-galactoside-specific lectin I
    Viscumin
    Cleaved into the following 2 chains:
    Alternative name(s):
    Beta-galactoside-specific lectin I chain A isoform 1
    ML-I A
    Short name:
    MLA
    rRNA N-glycosidase
    Alternative name(s):
    Beta-galactoside-specific lectin I chain B
    ML-I B
    Short name:
    MLB
    OrganismiViscum album (European mistletoe)
    Taxonomic identifieri3972 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeSantalalesViscaceaeViscum

    Pathology & Biotechi

    Pharmaceutical usei

    Due to its immunomodulative effects it is being studied in clinical trials in cancer patients as it may slow the growth of cancer cells and be an effective treatment for solid tumors.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 33333 PublicationsAdd
    BLAST
    Chaini34 – 287254Beta-galactoside-specific lectin 1 chain A isoform 1PRO_0000030749Add
    BLAST
    Propeptidei288 – 30114Connecting peptide1 PublicationPRO_0000030750Add
    BLAST
    Chaini302 – 564263Beta-galactoside-specific lectin 1 chain BPRO_0000030751Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi145 – 1451N-linked (GlcNAc...)1 Publication
    Disulfide bondi280 ↔ 306Interchain (between A and B chains)1 PublicationPROSITE-ProRule annotation
    Glycosylationi362 – 3621N-linked (GlcNAc...)1 Publication
    Disulfide bondi365 ↔ 3821 PublicationPROSITE-ProRule annotation
    Glycosylationi397 – 3971N-linked (GlcNAc...)1 Publication
    Glycosylationi437 – 4371N-linked (GlcNAc...)1 Publication
    Disulfide bondi453 ↔ 4661 PublicationPROSITE-ProRule annotation
    Disulfide bondi492 ↔ 5091 PublicationPROSITE-ProRule annotation

    Post-translational modificationi

    The A chain of variant MLA' is not glycosylated.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Disulfide-linked dimer of A and B chains.3 Publications

    Protein-protein interaction databases

    MINTiMINT-364969.

    Structurei

    Secondary structure

    1
    564
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi35 – 428
    Helixi47 – 6115
    Beta strandi62 – 676
    Beta strandi70 – 734
    Beta strandi80 – 823
    Beta strandi85 – 939
    Beta strandi98 – 1047
    Turni105 – 1073
    Beta strandi110 – 1156
    Beta strandi118 – 1214
    Helixi129 – 1313
    Beta strandi137 – 1415
    Helixi148 – 1558
    Helixi158 – 1603
    Helixi165 – 17612
    Helixi182 – 19514
    Helixi197 – 2015
    Helixi203 – 21513
    Helixi223 – 24018
    Beta strandi246 – 25510
    Turni256 – 2583
    Beta strandi259 – 2657
    Helixi266 – 2683
    Turni269 – 2724
    Beta strandi315 – 3173
    Helixi318 – 3203
    Beta strandi322 – 3254
    Helixi326 – 3283
    Beta strandi335 – 3395
    Helixi347 – 3493
    Beta strandi351 – 3533
    Beta strandi359 – 3613
    Beta strandi364 – 3696
    Beta strandi376 – 3816
    Turni382 – 3843
    Helixi387 – 3904
    Beta strandi400 – 4023
    Turni403 – 4064
    Beta strandi407 – 4104
    Beta strandi421 – 4233
    Helixi429 – 4313
    Beta strandi434 – 4374
    Beta strandi442 – 4476
    Helixi449 – 4513
    Beta strandi453 – 4575
    Beta strandi460 – 4645
    Helixi471 – 4733
    Beta strandi475 – 4773
    Beta strandi483 – 4853
    Beta strandi491 – 4944
    Beta strandi505 – 5095
    Helixi514 – 5163
    Beta strandi518 – 5203
    Beta strandi526 – 5283
    Turni529 – 5313
    Beta strandi534 – 5374
    Helixi538 – 5403
    Helixi542 – 5443
    Beta strandi547 – 5504
    Helixi556 – 5583
    Beta strandi561 – 5633

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1M2TX-ray1.89A34-287[»]
    B313-564[»]
    1ONKX-ray2.10A34-287[»]
    B302-563[»]
    1OQLX-ray3.00A34-282[»]
    B302-564[»]
    1PUMX-ray2.30A44-282[»]
    B302-564[»]
    1PUUX-ray2.30A44-282[»]
    B302-564[»]
    1SZ6X-ray2.05A44-282[»]
    B302-564[»]
    2R9KX-ray2.70A34-287[»]
    B302-564[»]
    2RG9X-ray1.95A44-282[»]
    B302-564[»]
    3D7WX-ray2.49A34-287[»]
    B302-564[»]
    3O5WX-ray2.70A34-287[»]
    B302-564[»]
    4EB2X-ray1.94A44-282[»]
    B302-564[»]
    4JKXX-ray2.35A34-282[»]
    B302-564[»]
    ProteinModelPortaliP81446.
    SMRiP81446. Positions 34-281, 302-563.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP81446.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini309 – 436128Ricin B-type lectin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini440 – 564125Ricin B-type lectin 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni324 – 3263Galactose binding
    Regioni536 – 5383Galactose binding

    Sequence similaritiesi

    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.
    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.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P81446-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNGHLASRRA WVWYFLMLGQ VFGATVKAET KFSYERLRLR VTHQTTGEEY    50
    FRFITLLRDY VSSGSFSNEI PLLRQSTIPV SDAQRFVLVE LTNEGGDSIT 100
    AAIDVTNLYV VAYQAGDQSY FLRDAPRGAE THLFTGTTRS SLPFNGSYPD 150
    LERYAGHRDQ IPLGIDQLIQ SVTALRFPGG STRTQARSIL ILIQMISEAA 200
    RFNPILWRAR QYINSGASFL PDVYMLELET SWGQQSTQVQ QSTDGVFNNP 250
    IRLAIPPGNF VTLTNVRDVI ASLAIMLFVC GERPSSSDVR YWPLVIRPVI 300
    ADDVTCSASE PTVRIVGRNG MCVDVRDDDF HDGNQIQLWP SKSNNDPNQL 350
    WTIKRDGTIR SNGSCLTTYG YTAGVYVMIF DCNTAVREAT LWEIWGNGTI 400
    INPRSNLVLA ASSGIKGTTL TVQTLDYTLG QGWLAGNDTA PREVTIYGFR 450
    DLCMESNGGS VWVETCVISQ QNQRWALYGD GSIRPKQNQD QCLTCGRDSV 500
    STVINIVSCS AGSSGQRWVF TNEGAILNLK NGLAMDVAQA NPKLRRIIIY 550
    PATGKPNQMW LPVP 564
    Length:564
    Mass (Da):62,628
    Last modified:April 17, 2007 - v3
    Checksum:i8BC06110DD458A6E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31G → A in AAR25545. (PubMed:15182350)Curated
    Sequence conflicti19 – 202GQ → CL in AAR25545. (PubMed:15182350)Curated
    Sequence conflicti37 – 371L → I in AAR25546. (PubMed:15182350)Curated
    Sequence conflicti62 – 621S → G AA sequence (PubMed:1450445)Curated
    Sequence conflicti83 – 831A → T in AAR25546. (PubMed:15182350)Curated
    Sequence conflicti92 – 921T → S in AAR25546. (PubMed:15182350)Curated
    Sequence conflicti94 – 941E → Q in AAR25545. (PubMed:15182350)Curated
    Sequence conflicti94 – 941E → Q AA sequence (PubMed:8980141)Curated
    Sequence conflicti94 – 941E → Q(PubMed:12823544)Curated
    Sequence conflicti96 – 961G → Q AA sequence (PubMed:8980141)Curated
    Sequence conflicti99 – 991I → V AA sequence (PubMed:8980141)Curated
    Sequence conflicti108 – 1081L → A AA sequence (PubMed:8980141)Curated
    Sequence conflicti117 – 1171D → N in AAR25546. (PubMed:15182350)Curated
    Sequence conflicti141 – 1411S → P in AAR25546. (PubMed:15182350)Curated
    Sequence conflicti181 – 1811S → N in AAL87006. (PubMed:15001393)Curated
    Sequence conflicti190 – 1901L → I in AAR25545. (PubMed:15182350)Curated
    Sequence conflicti190 – 1901L → I in AAR25546. (PubMed:15182350)Curated
    Sequence conflicti193 – 1931I → V in AAR25545. (PubMed:15182350)Curated
    Sequence conflicti193 – 1931I → V in AAR25546. (PubMed:15182350)Curated
    Sequence conflicti209 – 2091A → L in AAR25546. (PubMed:15182350)Curated
    Sequence conflicti209 – 2091A → Y AA sequence (PubMed:8980141)Curated
    Sequence conflicti241 – 2411Q → H AA sequence (PubMed:8980141)Curated
    Sequence conflicti241 – 2411Q → H(PubMed:12823544)Curated
    Sequence conflicti244 – 2441D → E in AAL87006. (PubMed:15001393)Curated
    Sequence conflicti322 – 3221C → R AA sequence (PubMed:9618256)Curated
    Sequence conflicti391 – 3933LWE → IWQ in AAR25545. (PubMed:15182350)Curated
    Sequence conflicti391 – 3933LWE → IWQ in AAL87006. (PubMed:15001393)Curated
    Sequence conflicti391 – 3933LWE → IWQ AA sequence (PubMed:9618256)Curated
    Sequence conflicti396 – 3961G → D AA sequence (PubMed:9618256)Curated
    Sequence conflicti408 – 4081V → A in AAL87006. (PubMed:15001393)Curated
    Sequence conflicti467 – 4671V → D AA sequence (PubMed:9618256)Curated
    Sequence conflicti468 – 4681I → S in AAR25545. (PubMed:15182350)Curated
    Sequence conflicti468 – 4681I → S in AAL87006. (PubMed:15001393)Curated
    Sequence conflicti468 – 4681I → S AA sequence (PubMed:9618256)Curated
    Sequence conflicti471 – 4744QNQR → KNQGK AA sequence (PubMed:9618256)Curated
    Sequence conflicti495 – 4951C → S AA sequence (PubMed:9618256)Curated
    Sequence conflicti511 – 5155AGSSG → GASGS AA sequence (PubMed:9618256)Curated
    Sequence conflicti538 – 5403AQA → KGS in AAL87006. (PubMed:15001393)Curated
    Sequence conflicti546 – 5461R → Q in AAL87006. (PubMed:15001393)Curated
    Sequence conflicti564 – 5641P → F AA sequence (PubMed:9618256)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti48 – 481E → D in MLA'. 1 Publication
    Natural varianti145 – 1451N → T in MLA'. 1 Publication
    Natural varianti149 – 1491P → T in MLA'. 1 Publication
    Natural varianti166 – 1672DQ → EE in MLA'.
    Natural varianti173 – 1731T → S in MLA'. 1 Publication
    Natural varianti177 – 1771F → Y in MLA'. 1 Publication
    Natural varianti184 – 1841T → A in MLA'. 1 Publication
    Natural varianti212 – 2121Y → D in MLA'. 1 Publication
    Natural varianti217 – 2171A → E in MLA'. 1 Publication
    Natural varianti223 – 2231V → M in MLA'. 1 Publication
    Natural varianti251 – 2511I → F in MLA'. 1 Publication
    Natural varianti256 – 2572PP → ST in MLA'.
    Natural varianti264 – 2641T → S in MLA'. 1 Publication
    Natural varianti268 – 2681D → S in MLA'. 1 Publication
    Natural varianti319 – 3191N → S.1 Publication
    Natural varianti357 – 3571G → N.1 Publication
    Natural varianti458 – 4581G → Q.1 Publication
    Natural varianti495 – 4951C → V.1 Publication
    Natural varianti524 – 5241G → Y.1 Publication
    Natural varianti531 – 5333NGL → KGP.
    Natural varianti531 – 5311N → S.1 Publication
    Natural varianti531 – 5311N → T.1 Publication
    Natural varianti532 – 5354GLAM → SLMV.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY377890 Genomic DNA. Translation: AAR25545.1.
    AY377891 mRNA. Translation: AAR25546.1.
    AY081149 mRNA. Translation: AAL87006.1.
    PIRiJW0090.
    PD0018.
    PD0019.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY377890 Genomic DNA. Translation: AAR25545.1 .
    AY377891 mRNA. Translation: AAR25546.1 .
    AY081149 mRNA. Translation: AAL87006.1 .
    PIRi JW0090.
    PD0018.
    PD0019.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1M2T X-ray 1.89 A 34-287 [» ]
    B 313-564 [» ]
    1ONK X-ray 2.10 A 34-287 [» ]
    B 302-563 [» ]
    1OQL X-ray 3.00 A 34-282 [» ]
    B 302-564 [» ]
    1PUM X-ray 2.30 A 44-282 [» ]
    B 302-564 [» ]
    1PUU X-ray 2.30 A 44-282 [» ]
    B 302-564 [» ]
    1SZ6 X-ray 2.05 A 44-282 [» ]
    B 302-564 [» ]
    2R9K X-ray 2.70 A 34-287 [» ]
    B 302-564 [» ]
    2RG9 X-ray 1.95 A 44-282 [» ]
    B 302-564 [» ]
    3D7W X-ray 2.49 A 34-287 [» ]
    B 302-564 [» ]
    3O5W X-ray 2.70 A 34-287 [» ]
    B 302-564 [» ]
    4EB2 X-ray 1.94 A 44-282 [» ]
    B 302-564 [» ]
    4JKX X-ray 2.35 A 34-282 [» ]
    B 302-564 [» ]
    ProteinModelPortali P81446.
    SMRi P81446. Positions 34-281, 302-563.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-364969.

    Protein family/group databases

    CAZyi CBM13. Carbohydrate-Binding Module Family 13.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P81446.

    Family and domain databases

    Gene3Di 3.40.420.10. 1 hit.
    4.10.470.10. 1 hit.
    InterProi IPR001574. Ribosome_inactivat_prot.
    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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of the genes encoding toxic lectins in mistletoe (Viscum album L)."
      Kourmanova A.G., Soudarkina O.J., Olsnes S., Kozlov J.V.
      Eur. J. Biochem. 271:2350-2360(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION.
      Tissue: Leaf.
    2. "Purification and characterization of four isoforms of Himalayan mistletoe ribosome-inactivating protein from Viscum album having unique sugar affinity."
      Mishra V., Sharma R.S., Yadav S., Babu C.R., Singh T.P.
      Arch. Biochem. Biophys. 423:288-301(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 34-564, PROTEIN SEQUENCE OF 34-53, FUNCTION.
      Tissue: Leaf.
    3. "Complete amino acid sequence of the A chain of mistletoe lectin I."
      Soler M.H., Stoeva S., Schwamborn C., Wilhelm S., Stiefel T., Voelter W.
      FEBS Lett. 399:153-157(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 34-287 (CHAIN A), VARIANTS ASP-48; THR-145; THR-149; 166-GLU-GLU-167; SER-173; TYR-177; ALA-184; ASP-212; GLU-217; MET-223; PHE-251; 256-SER-THR-257; SER-264 AND SER-268.
    4. "Identity of the N-terminal sequences of the three A chains of mistletoe (Viscum album L.) lectins: homology with ricin-like plant toxins and single-chain ribosome-inhibiting proteins."
      Dietrich J.B., Ribereau-Gayon G., Jung M.L., Franz H., Beck J.P., Anton R.
      Anticancer Drugs 3:507-511(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 34-62, FUNCTION.
    5. "Complete amino acid sequence of the B chain of mistletoe lectin I."
      Soler M.H., Stoeva S., Voelter W.
      Biochem. Biophys. Res. Commun. 246:596-601(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 302-564 (CHAIN B), VARIANTS SER-319; ASN-357; GLN-458; VAL-495; TYR-524; SER-531; THR-531; 531-LYS--PRO-533 AND 532-SER--VAL-535.
    6. "Primary structure and molecular modeling of mistletoe lectin I from Viscum album."
      Eschenburg S., Krauspenhaar R., Mikhailov A., Stoeva S., Betzel C., Voelter W.
      Biochem. Biophys. Res. Commun. 247:367-372(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING OF 34-287 AND 302-564.
    7. "Crystallisation under microgravity of mistletoe lectin I from Viscum album with adenine monophosphate and the crystal structure at 1.9 A resolution."
      Krauspenhaar R., Rypniewski W., Kalkura N., Moore K., DeLucas L., Stoeva S., Mikhailov A., Voelter W., Betzel C.
      Acta Crystallogr. D 58:1704-1707(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 34-287 AND 302-564 IN COMPLEX WITH AMP.
    8. "Crystal structure at 3 A of mistletoe lectin I, a dimeric type-II ribosome-inactivating protein, complexed with galactose."
      Niwa H., Tonevitsky A.G., Agapov I.I., Saward S., Pfueller U., Palmer R.A.
      Eur. J. Biochem. 270:2739-2749(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 34-282 AND 302-564 IN COMPLEX WITH GALACTOSE, SUBUNIT, GLYCOSYLATION AT ASN-145; ASN-362; ASN-397 AND ASN-437, DISULFIDE BONDS.
    9. "Mistletoe lectin I in complex with galactose and lactose reveals distinct sugar-binding properties."
      Mikeska R., Wacker R., Arni R., Singh T.P., Mikhailov A., Gabdoulkhakov A., Voelter W., Betzel C.
      Acta Crystallogr. F 61:17-25(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 34-282 AND 302-564 IN COMPLEX WITH LACTOSE AND GALACTOSE.
    10. "Mistletoe lectin I From Viscum album."
      Gabdoulkhakov A.G., Savoshkina Y., Krauspenhaar R., Stoeva S., Konareva N., Kornilov V., Kornev A.N., Voelter W., Nikonov S.V., Betzel C., Mikhailov A.M.
      Submitted (FEB-2003) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 34-287 AND 302-563.

    Entry informationi

    Entry nameiML1_VISAL
    AccessioniPrimary (citable) accession number: P81446
    Secondary accession number(s): P81830
    , Q6H270, Q6H271, Q8RXH6, Q9S7D0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: April 17, 2007
    Last modified: October 1, 2014
    This is version 99 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Several isoforms exist.

    Keywords - Technical termi

    3D-structure, Direct protein sequencing, Pharmaceutical

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3