2Y6I
Crystal Structure of Collagenase G from Clostridium histolyticum in complex with Isoamylphosphonyl-Gly-Pro-Ala at 3.25 Angstrom Resolution
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 1791 |
| Chain | Residue |
| A | HIS523 |
| A | HIS527 |
| A | GLU555 |
| A | HOH2042 |
| B | IPI1 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FLC A 1793 |
| Chain | Residue |
| A | ASP737 |
| A | SER740 |
| A | LYS741 |
| A | SER568 |
| A | TYR618 |
| A | MET622 |
| A | TRP736 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE TRS A 1794 |
| Chain | Residue |
| A | LYS247 |
| A | ASN251 |
| A | LYS291 |
| A | PHE295 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE TRS A 1795 |
| Chain | Residue |
| A | THR565 |
| A | ARG566 |
| A | THR567 |
| A | SER568 |
| A | LEU675 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE TRS A 1796 |
| Chain | Residue |
| A | ASP368 |
| A | HOH2043 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG A 1797 |
| Chain | Residue |
| A | ALA458 |
| A | LEU459 |
| A | ASN634 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE PEG A 1798 |
| Chain | Residue |
| A | GLU619 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 1PE A 1799 |
| Chain | Residue |
| A | ALA277 |
| A | PRO278 |
| A | ASP279 |
| A | THR284 |
| A | TRP337 |
| A | ASP340 |
| A | HOH2044 |
Functional Information from PROSITE/UniProt
| site_id | PS00142 |
| Number of Residues | 10 |
| Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. LFRHEYTHYL |
| Chain | Residue | Details |
| A | LEU520-LEU529 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 269 |
| Details | Region: {"description":"Activator domain required for full activity on collagen","evidences":[{"source":"PubMed","id":"21947205","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23703618","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 111 |
| Details | Region: {"description":"Helper subdomain","evidences":[{"source":"PubMed","id":"23703618","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11121400","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q899Y1","evidenceCode":"ECO:0000250"},{"source":"PubMed","id":"23703618","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21947205","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23703618","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2Y50","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2Y6I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ARE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21947205","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23703618","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2Y50","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2Y6I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ARE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
