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 | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 320 |
Chain | Residue |
A | HIS142 |
A | HIS146 |
A | GLU166 |
A | TI2317 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 321 |
Chain | Residue |
A | ASP185 |
A | GLU187 |
A | GLU190 |
A | HOH327 |
A | ASP138 |
A | GLU177 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA A 322 |
Chain | Residue |
A | GLU177 |
A | LYS182 |
A | ASN183 |
A | ASP185 |
A | GLU190 |
A | HOH348 |
A | HOH351 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 323 |
Chain | Residue |
A | ASP57 |
A | ASP59 |
A | GLN61 |
A | HOH329 |
A | HOH343 |
A | HOH379 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 324 |
Chain | Residue |
A | TYR193 |
A | THR194 |
A | ILE197 |
A | ASP200 |
A | HOH335 |
A | HOH384 |
site_id | AC6 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE TI2 A 317 |
Chain | Residue |
A | ASN111 |
A | ASN112 |
A | ALA113 |
A | PHE114 |
A | VAL139 |
A | HIS142 |
A | GLU143 |
A | HIS146 |
A | TYR157 |
A | GLU166 |
A | ILE188 |
A | GLY189 |
A | LEU202 |
A | ARG203 |
A | HIS231 |
A | ZN320 |
A | HOH393 |
A | HOH416 |
A | HOH457 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE DMS A 325 |
Chain | Residue |
A | HIS146 |
A | HOH352 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DMS A 326 |
Chain | Residue |
A | HIS216 |
A | SER218 |
A | TYR251 |
site_id | ZN |
Number of Residues | 3 |
Details | ZN BINDING SITE |
Chain | Residue |
A | HIS146 |
A | HIS142 |
A | GLU166 |
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
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 | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1tlp |
Chain | Residue | Details |
A | HIS231 | |
A | GLU143 | |
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 |