Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006508 | biological_process | proteolysis |
A | 0008235 | molecular_function | metalloexopeptidase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN A 292 |
Chain | Residue |
A | ASP117 |
A | GLU152 |
A | HIS256 |
A | ZN293 |
A | HOH599 |
A | HOH601 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN A 293 |
Chain | Residue |
A | ASP179 |
A | ZN292 |
A | HOH599 |
A | HIS97 |
A | ASP117 |
A | GLU151 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE NA A 294 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA A 295 |
Chain | Residue |
A | GLY24 |
A | SER27 |
A | SER28 |
A | ASN200 |
A | HOH378 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA A 296 |
Chain | Residue |
A | THR38 |
A | TYR73 |
A | ASN74 |
A | HOH396 |
A | HOH636 |
site_id | AC6 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE NA A 297 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA A 298 |
Chain | Residue |
A | THR257 |
A | THR258 |
A | THR258 |
A | GLN259 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NA A 299 |
Chain | Residue |
A | LEU213 |
A | PRO214 |
A | SER215 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NA A 300 |
Chain | Residue |
A | ALA19 |
A | LYS273 |
A | HOH459 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SCN A 301 |
Chain | Residue |
A | THR194 |
A | SER199 |
A | THR202 |
A | GLN203 |
A | LEU262 |
A | HOH322 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SCN A 302 |
Chain | Residue |
A | GLN7 |
A | ALA12 |
A | TRP13 |
A | GLN16 |
A | HOH395 |
A | HOH609 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10413478, ECO:0000269|PubMed:11401547, ECO:0000269|PubMed:8087555, ECO:0000269|PubMed:8647077, ECO:0007744|PDB:1AMP, ECO:0007744|PDB:1CP6, ECO:0007744|PDB:1FT7, ECO:0007744|PDB:1IGB, ECO:0007744|PDB:1LOK, ECO:0007744|PDB:1RTQ, ECO:0007744|PDB:1TXR, ECO:0007744|PDB:1XRY, ECO:0007744|PDB:2ANP, ECO:0007744|PDB:2DEA, ECO:0007744|PDB:2IQ6, ECO:0007744|PDB:2NYQ, ECO:0007744|PDB:3B35, ECO:0007744|PDB:3B3C, ECO:0007744|PDB:3B3S, ECO:0007744|PDB:3B3T, ECO:0007744|PDB:3B3V, ECO:0007744|PDB:3B3W, ECO:0007744|PDB:3B7I, ECO:0007744|PDB:3FH4, ECO:0007744|PDB:3VH9 |
Chain | Residue | Details |
A | HIS97 | |
A | ASP117 | |
A | GLU152 | |
A | ASP179 | |
A | HIS256 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1amp |
Chain | Residue | Details |
A | GLU151 | |
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 167 |
Chain | Residue | Details |
A | HIS97 | metal ligand |
A | ASP117 | metal ligand |
A | GLU151 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | GLU152 | metal ligand |
A | ASP179 | metal ligand |
A | HIS256 | metal ligand |