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 321 |
Chain | Residue |
A | HIS142 |
A | HIS146 |
A | GLU166 |
A | CL326 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 322 |
Chain | Residue |
A | HOH395 |
A | ASP57 |
A | ASP59 |
A | GLN61 |
A | HOH367 |
A | HOH382 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 323 |
Chain | Residue |
A | ASP138 |
A | GLU177 |
A | ASP185 |
A | GLU187 |
A | GLU190 |
A | HOH358 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 324 |
Chain | Residue |
A | TYR193 |
A | THR194 |
A | ILE197 |
A | ASP200 |
A | HOH339 |
A | HOH356 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 325 |
Chain | Residue |
A | GLY12 |
A | LEU14 |
A | ASP16 |
A | LYS18 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A 326 |
Chain | Residue |
A | HIS142 |
A | TYR157 |
A | GLU166 |
A | HIS231 |
A | ZN321 |
site_id | AC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL A 327 |
site_id | AC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL A 328 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 329 |
Chain | Residue |
A | ARG285 |
A | LYS307 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 330 |
Chain | Residue |
A | ARG260 |
A | ASP261 |
A | HOH398 |
site_id | BC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL A 331 |
site_id | BC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 333 |
Chain | Residue |
A | GLY3 |
A | THR4 |
A | SER5 |
A | TYR28 |
A | ASN60 |
A | HOH352 |
A | HOH394 |
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 | 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 |