4GAA
Structure of Leukotriene A4 hydrolase from Xenopus laevis complexed with inhibitor bestatin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004177 | molecular_function | aminopeptidase activity |
| A | 0004301 | molecular_function | epoxide hydrolase activity |
| A | 0004463 | molecular_function | leukotriene-A4 hydrolase activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006508 | biological_process | proteolysis |
| A | 0008237 | molecular_function | metallopeptidase activity |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0019370 | biological_process | leukotriene biosynthetic process |
| A | 0043171 | biological_process | peptide catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004177 | molecular_function | aminopeptidase activity |
| B | 0004301 | molecular_function | epoxide hydrolase activity |
| B | 0004463 | molecular_function | leukotriene-A4 hydrolase activity |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006508 | biological_process | proteolysis |
| B | 0008237 | molecular_function | metallopeptidase activity |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0019370 | biological_process | leukotriene biosynthetic process |
| B | 0043171 | biological_process | peptide catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 701 |
| Chain | Residue |
| A | HIS292 |
| A | HIS296 |
| A | GLU315 |
| A | BES702 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE BES A 702 |
| Chain | Residue |
| A | GLU268 |
| A | HIS292 |
| A | GLU293 |
| A | HIS296 |
| A | GLU315 |
| A | PHE375 |
| A | TYR380 |
| A | ARG560 |
| A | ZN701 |
| A | HOH836 |
| A | GLN133 |
| A | TYR264 |
| A | GLY265 |
| A | GLY266 |
| A | MET267 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 701 |
| Chain | Residue |
| B | HIS292 |
| B | HIS296 |
| B | GLU315 |
| B | BES702 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE BES B 702 |
| Chain | Residue |
| B | GLN131 |
| B | GLN133 |
| B | TYR264 |
| B | GLY265 |
| B | GLY266 |
| B | GLU268 |
| B | HIS292 |
| B | GLU293 |
| B | HIS296 |
| B | GLU315 |
| B | PHE375 |
| B | TYR380 |
| B | ARG560 |
| B | ZN701 |
Functional Information from PROSITE/UniProt
| site_id | PS00142 |
| Number of Residues | 10 |
| Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VIAHEISHSW |
| Chain | Residue | Details |
| A | VAL289-TRP298 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PIRSR:PIRSR634015-1 |
| Chain | Residue | Details |
| A | GLU293 | |
| B | GLU293 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000255|PIRSR:PIRSR634015-1 |
| Chain | Residue | Details |
| A | TYR380 | |
| B | TYR380 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P09960 |
| Chain | Residue | Details |
| A | GLN131 | |
| A | PRO263 | |
| A | ARG560 | |
| B | GLN131 | |
| B | PRO263 | |
| B | ARG560 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|PIRSR:PIRSR634015-3, ECO:0000269|PubMed:24333438, ECO:0007744|PDB:4GAA |
| Chain | Residue | Details |
| A | HIS292 | |
| A | HIS296 | |
| A | GLU315 | |
| B | HIS292 | |
| B | HIS296 | |
| B | GLU315 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | SITE: Pro-Gly-Pro binding => ECO:0000250|UniProtKB:P09960 |
| Chain | Residue | Details |
| A | GLU268 | |
| A | GLY559 | |
| B | GLU268 | |
| B | GLY559 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | SITE: Essential for epoxide hydrolase activity, but not for aminopeptidase activity => ECO:0000250|UniProtKB:P09960 |
| Chain | Residue | Details |
| A | ASP372 | |
| B | ASP372 |
