2E3X
Crystal structure of Russell's viper venom metalloproteinase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004222 | molecular_function | metalloendopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| A | 0008237 | molecular_function | metallopeptidase activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0035821 | biological_process | modulation of process of another organism |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0090729 | molecular_function | toxin activity |
| C | 0005576 | cellular_component | extracellular region |
| C | 0035821 | biological_process | modulation of process of another organism |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0090729 | molecular_function | toxin activity |
Functional Information from PROSITE/UniProt
| site_id | PS00142 |
| Number of Residues | 10 |
| Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. IMAHELSHNL |
| Chain | Residue | Details |
| A | ILE142-LEU151 |
| site_id | PS00427 |
| Number of Residues | 20 |
| Details | DISINTEGRIN_1 Disintegrins signature. CgnGlCCy.QCkIktagtvCR |
| Chain | Residue | Details |
| A | CYS253-ARG272 |
| site_id | PS00615 |
| Number of Residues | 26 |
| Details | C_TYPE_LECTIN_1 C-type lectin domain signature. CFvlekesgyrm..WFNRNCeeryl.FVC |
| Chain | Residue | Details |
| B | CYS102-CYS127 | |
| C | CYS98-CYS121 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 194 |
| Details | Domain: {"description":"Peptidase M12B","evidences":[{"source":"PROSITE-ProRule","id":"PRU00276","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 86 |
| Details | Domain: {"description":"Disintegrin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00068","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Motif: {"description":"D/ECD-tripeptide"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00276","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 14 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"8144654","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"18060879","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8144654","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"18060879","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 111 |
| Details | Domain: {"description":"C-type lectin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00040","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
