Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004222 | molecular_function | metalloendopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 401 |
| Chain | Residue |
| A | ASP138 |
| A | GLU177 |
| A | ASP185 |
| A | GLU187 |
| A | GLU190 |
| A | HOH525 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue CA A 402 |
| Chain | Residue |
| A | GLU190 |
| A | HOH562 |
| A | GLU177 |
| A | ASN183 |
| A | ASP185 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 403 |
| Chain | Residue |
| A | ASP57 |
| A | ASP59 |
| A | GLN61 |
| A | HOH507 |
| A | HOH523 |
| A | HOH589 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 404 |
| Chain | Residue |
| A | TYR193 |
| A | THR194 |
| A | ILE197 |
| A | ASP200 |
| A | HOH505 |
| A | HOH544 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 405 |
| Chain | Residue |
| A | HIS142 |
| A | HIS146 |
| A | GLU166 |
| A | PO4408 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue VAL A 1001 |
| Chain | Residue |
| A | ASN112 |
| A | ALA113 |
| A | GLU143 |
| A | ARG203 |
| A | HIS231 |
| A | LYS1002 |
| A | PO4408 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue LYS A 1002 |
| Chain | Residue |
| A | ASN111 |
| A | ASN112 |
| A | HIS231 |
| A | VAL1001 |
| A | HOH528 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | binding site for residue PO4 A 408 |
| Chain | Residue |
| A | ALA113 |
| A | HIS142 |
| A | GLU143 |
| A | HIS146 |
| A | TYR157 |
| A | GLU166 |
| A | HIS231 |
| A | ZN405 |
| A | VAL1001 |
| A | HOH503 |
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 |
| A | VAL139-VAL148 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | GLU143 | |
| Chain | Residue | Details |
| A | HIS231 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP57 | |
| A | ASP185 | |
| A | GLU187 | |
| A | GLU190 | |
| A | TYR193 | |
| A | THR194 | |
| A | ILE197 | |
| A | ASP200 | |
| A | ASP59 | |
| A | GLN61 | |
| A | ASP138 | |
| A | HIS142 | |
| A | HIS146 | |
| A | GLU166 | |
| A | GLU177 | |
| A | ASN183 | |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 176 |
| Chain | Residue | Details |
| A | HIS142 | metal ligand |
| A | GLU143 | electrostatic stabiliser, metal ligand |
| A | HIS146 | metal ligand |
| A | TYR157 | electrostatic stabiliser, hydrogen bond donor, steric role |
| A | GLU166 | metal ligand |
| A | ASP226 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| A | HIS231 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
