Functional Information from GO Data
| Chain | GOid | namespace | contents |
| E | 0004222 | molecular_function | metalloendopeptidase activity |
| E | 0006508 | biological_process | proteolysis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN E 401 |
| Chain | Residue |
| E | HIS142 |
| E | HIS146 |
| E | GLU166 |
| E | 2GC413 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA E 402 |
| Chain | Residue |
| E | HOH501 |
| E | ASP138 |
| E | GLU177 |
| E | ASP185 |
| E | GLU187 |
| E | GLU190 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA E 403 |
| Chain | Residue |
| E | ASP57 |
| E | ASP59 |
| E | GLN61 |
| E | HOH516 |
| E | HOH530 |
| E | HOH873 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA E 404 |
| Chain | Residue |
| E | TYR193 |
| E | THR194 |
| E | ILE197 |
| E | ASP200 |
| E | HOH539 |
| E | HOH595 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA E 405 |
| Chain | Residue |
| E | GLU177 |
| E | ASN183 |
| E | ASP185 |
| E | GLU190 |
| E | HOH564 |
| E | HOH872 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE DMS E 406 |
| Chain | Residue |
| E | ILE1 |
| E | THR2 |
| E | GLY3 |
| E | GLN31 |
| E | ASN33 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE DMS E 407 |
| Chain | Residue |
| E | TYR110 |
| E | ASN112 |
| E | PHE114 |
| E | 2GC413 |
| E | 2GC413 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE DMS E 408 |
| Chain | Residue |
| E | GLY95 |
| E | PRO184 |
| E | TRP186 |
| E | HOH578 |
| E | HOH730 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE DMS E 409 |
| Chain | Residue |
| E | TYR66 |
| E | HIS216 |
| E | SER218 |
| E | TYR251 |
| E | HOH566 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL E 410 |
| Chain | Residue |
| E | GLY109 |
| E | TYR110 |
| E | ASN111 |
| E | ASN112 |
| E | HOH662 |
| E | HOH691 |
| E | HOH931 |
| E | HOH933 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL E 411 |
| Chain | Residue |
| E | PHE114 |
| E | TRP115 |
| E | HIS146 |
| E | TYR157 |
| E | 2GC413 |
| E | HOH517 |
| E | HOH557 |
| E | HOH827 |
| site_id | BC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GOL E 412 |
| Chain | Residue |
| E | GLY247 |
| E | GLY248 |
| E | THR249 |
| E | VAL255 |
| E | GLN273 |
| E | TYR274 |
| E | LEU275 |
| E | THR276 |
| E | HOH551 |
| E | HOH594 |
| E | HOH607 |
| E | HOH629 |
| site_id | BC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE 2GC E 413 |
| Chain | Residue |
| E | TYR106 |
| E | ASN112 |
| E | ALA113 |
| E | PHE114 |
| E | TRP115 |
| E | VAL139 |
| E | HIS142 |
| E | GLU143 |
| E | HIS146 |
| E | TYR157 |
| E | GLU166 |
| E | LEU202 |
| E | ARG203 |
| E | HIS231 |
| E | ZN401 |
| E | DMS407 |
| E | DMS407 |
| E | GOL411 |
| E | HOH575 |
| E | HOH892 |
| E | HOH933 |
Functional Information from PROSITE/UniProt
| site_id | PS00142 |
| Number of Residues | 10 |
| Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VVAHELTHAV |
| Chain | Residue | Details |
| E | VAL139-VAL148 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"4808703","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"4808703","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {} |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 176 |