Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004222 | molecular_function | metalloendopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| A | 0008270 | molecular_function | zinc ion binding |
| B | 0004222 | molecular_function | metalloendopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| B | 0008270 | molecular_function | zinc ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 500 |
| Chain | Residue |
| A | HIS223 |
| A | HIS227 |
| A | GLU262 |
| A | GB4600 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 500 |
| Chain | Residue |
| B | HIS223 |
| B | HIS227 |
| B | GLU262 |
| B | GB4600 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GB4 A 600 |
| Chain | Residue |
| A | PHE163 |
| A | PHE194 |
| A | HIS223 |
| A | GLU224 |
| A | HIS227 |
| A | GLU262 |
| A | ARG363 |
| A | TYR366 |
| A | PHE369 |
| A | ZN500 |
| A | HOH1405 |
| A | ILE161 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GB4 B 600 |
| Chain | Residue |
| B | VAL70 |
| B | ILE161 |
| B | PHE163 |
| B | PHE194 |
| B | HIS223 |
| B | GLU224 |
| B | HIS227 |
| B | GLU262 |
| B | ARG363 |
| B | TYR366 |
| B | PHE369 |
| B | ZN500 |
Functional Information from PROSITE/UniProt
| site_id | PS00142 |
| Number of Residues | 10 |
| Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TLAHELIHAG |
| Chain | Residue | Details |
| A | THR220-GLY229 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1i1e |
| Chain | Residue | Details |
| A | GLU262 | |
| A | TYR366 | |
| A | ARG363 | |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1i1e |
| Chain | Residue | Details |
| B | GLU262 | |
| B | TYR366 | |
| B | ARG363 | |
