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 | HOH465 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 402 |
Chain | Residue |
A | GLU190 |
A | HOH493 |
A | HOH502 |
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 | HOH462 |
A | HOH470 |
A | HOH471 |
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 | HOH510 |
A | HOH524 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 405 |
Chain | Residue |
A | HIS142 |
A | GLU143 |
A | HIS146 |
A | GLU166 |
site_id | AC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE 0A9 A 406 |
Chain | Residue |
A | ASN112 |
A | ALA113 |
A | VAL139 |
A | GLU143 |
A | ILE188 |
A | LEU202 |
A | ARG203 |
A | HIS231 |
A | HOH354 |
A | HOH633 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE 0A9 A 407 |
Chain | Residue |
A | THR26 |
A | TYR29 |
A | TYR211 |
A | GLY212 |
A | ASP213 |
A | HOH394 |
A | 0A9408 |
A | HOH642 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE 0A9 A 408 |
Chain | Residue |
A | ILE1 |
A | SER25 |
A | TYR29 |
A | TYR211 |
A | GLY212 |
A | HOH360 |
A | 0A9407 |
A | HOH655 |
A | HOH745 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE DMS A 317 |
Chain | Residue |
A | TYR66 |
A | HIS216 |
A | SER218 |
A | HOH558 |
A | HOH660 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE DMS A 318 |
Chain | Residue |
A | ILE1 |
A | THR2 |
A | GLY3 |
A | GLN31 |
A | ASN33 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACT A 1428 |
Chain | Residue |
A | TYR24 |
A | TYR24 |
A | SER25 |
site_id | BC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE P6G A 319 |
Chain | Residue |
A | THR293 |
A | ASP294 |
A | TYR296 |
A | GLY297 |
A | GLY297 |
A | HOH361 |
A | HOH361 |
A | HOH570 |
A | HOH570 |
site_id | BC4 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE P6G A 320 |
Chain | Residue |
A | PHE178 |
A | TRP186 |
A | SER245 |
A | GLN246 |
A | GLY257 |
A | GLY259 |
A | ARG260 |
A | ASP261 |
A | GLN273 |
A | HOH457 |
A | HOH489 |
A | HOH609 |
A | HOH670 |
A | HOH766 |
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 |