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 | 18 |
Details | BINDING SITE FOR RESIDUE UBX A 401 |
Chain | Residue |
A | TYR106 |
A | GLU166 |
A | ARG203 |
A | HIS231 |
A | GOL404 |
A | DMS408 |
A | DMS408 |
A | ZN410 |
A | HOH703 |
A | HOH860 |
A | ASN112 |
A | ALA113 |
A | PHE114 |
A | TRP115 |
A | HIS142 |
A | GLU143 |
A | HIS146 |
A | TYR157 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 402 |
Chain | Residue |
A | SER65 |
A | TYR66 |
A | PRO69 |
A | HIS105 |
A | ASP124 |
A | HOH520 |
A | HOH849 |
site_id | AC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE GOL A 403 |
Chain | Residue |
A | GLY247 |
A | GLY248 |
A | THR249 |
A | VAL255 |
A | GLN273 |
A | LEU275 |
A | HOH619 |
A | HOH649 |
A | HOH737 |
A | HOH738 |
A | HOH759 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 404 |
Chain | Residue |
A | PHE114 |
A | TRP115 |
A | HIS146 |
A | TYR157 |
A | UBX401 |
A | HOH581 |
A | HOH596 |
A | HOH625 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 405 |
Chain | Residue |
A | GLY109 |
A | TYR110 |
A | ASN111 |
A | ASN112 |
A | GLN158 |
A | HOH519 |
A | HOH803 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE DMS A 406 |
Chain | Residue |
A | GLY95 |
A | PRO184 |
A | TRP186 |
A | HOH633 |
A | HOH689 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE DMS A 407 |
Chain | Residue |
A | TYR24 |
A | TYR24 |
A | SER25 |
A | TYR28 |
A | HOH503 |
A | HOH658 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE DMS A 408 |
Chain | Residue |
A | TYR110 |
A | ASN112 |
A | PHE114 |
A | UBX401 |
A | UBX401 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE DMS A 409 |
Chain | Residue |
A | THR2 |
A | GLY3 |
A | GLN31 |
A | ASN33 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 410 |
Chain | Residue |
A | HIS142 |
A | HIS146 |
A | GLU166 |
A | UBX401 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 411 |
Chain | Residue |
A | ASP138 |
A | GLU177 |
A | ASP185 |
A | GLU187 |
A | GLU190 |
A | HOH850 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 412 |
Chain | Residue |
A | GLU177 |
A | ASN183 |
A | ASP185 |
A | GLU190 |
A | HOH855 |
A | HOH856 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 413 |
Chain | Residue |
A | TYR193 |
A | THR194 |
A | ILE197 |
A | ASP200 |
A | HOH836 |
A | HOH852 |
site_id | BC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 414 |
Chain | Residue |
A | ASP57 |
A | ASP59 |
A | GLN61 |
A | HOH851 |
A | HOH853 |
A | HOH854 |
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 |