3B7R
Leukotriene A4 Hydrolase Complexed with Inhibitor RB3040
Functional Information from GO Data
Chain | GOid | namespace | contents |
L | 0003723 | molecular_function | RNA binding |
L | 0004177 | molecular_function | aminopeptidase activity |
L | 0004301 | molecular_function | epoxide hydrolase activity |
L | 0004463 | molecular_function | leukotriene-A4 hydrolase activity |
L | 0005515 | molecular_function | protein binding |
L | 0005576 | cellular_component | extracellular region |
L | 0005634 | cellular_component | nucleus |
L | 0005654 | cellular_component | nucleoplasm |
L | 0005737 | cellular_component | cytoplasm |
L | 0005829 | cellular_component | cytosol |
L | 0006508 | biological_process | proteolysis |
L | 0006629 | biological_process | lipid metabolic process |
L | 0006691 | biological_process | leukotriene metabolic process |
L | 0008233 | molecular_function | peptidase activity |
L | 0008237 | molecular_function | metallopeptidase activity |
L | 0008270 | molecular_function | zinc ion binding |
L | 0010043 | biological_process | response to zinc ion |
L | 0019370 | biological_process | leukotriene biosynthetic process |
L | 0019538 | biological_process | protein metabolic process |
L | 0043171 | biological_process | peptide catabolic process |
L | 0043434 | biological_process | response to peptide hormone |
L | 0045148 | molecular_function | tripeptide aminopeptidase activity |
L | 0046872 | molecular_function | metal ion binding |
L | 0060509 | biological_process | type I pneumocyte differentiation |
L | 0070006 | molecular_function | metalloaminopeptidase activity |
L | 0070062 | cellular_component | extracellular exosome |
L | 1904724 | cellular_component | tertiary granule lumen |
L | 1904813 | cellular_component | ficolin-1-rich granule lumen |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN L 701 |
Chain | Residue |
L | HIS295 |
L | HIS299 |
L | GLU318 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE YB L 801 |
Chain | Residue |
L | HOH1657 |
L | ASP47 |
L | ASP481 |
L | HOH1444 |
L | HOH1447 |
L | HOH1543 |
L | HOH1609 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE IMD L 802 |
Chain | Residue |
L | GLY344 |
L | GLY347 |
L | GLU348 |
L | ASN351 |
L | GLU501 |
L | ALA504 |
L | GLN508 |
site_id | AC4 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE BIR L 1001 |
Chain | Residue |
L | GLN136 |
L | TYR267 |
L | GLY268 |
L | GLY269 |
L | GLU271 |
L | ASN291 |
L | HIS295 |
L | GLU296 |
L | HIS299 |
L | GLU318 |
L | TYR378 |
L | TYR383 |
L | ARG563 |
L | LYS565 |
L | HOH1005 |
L | HOH1064 |
L | HOH1391 |
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 |
L | VAL292-TRP301 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:11675384, ECO:0000305|PubMed:12207002, ECO:0000305|PubMed:24591641, ECO:0007744|PDB:1H19 |
Chain | Residue | Details |
L | GLU296 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:11675384, ECO:0000305|PubMed:12207002, ECO:0000305|PubMed:24591641, ECO:0007744|PDB:1H19 |
Chain | Residue | Details |
L | TYR383 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18804029 |
Chain | Residue | Details |
L | GLN134 | |
L | PRO266 | |
L | ARG563 |
Chain | Residue | Details |
L | HIS295 | |
L | HIS299 |
Chain | Residue | Details |
L | GLU318 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | SITE: Pro-Gly-Pro binding => ECO:0000269|PubMed:24591641 |
Chain | Residue | Details |
L | GLU271 | |
L | GLY562 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | SITE: Essential for epoxide hydrolase activity, but not for aminopeptidase activity => ECO:0000269|PubMed:11917124 |
Chain | Residue | Details |
L | ASP375 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | SITE: Covalently modified during suicide inhibition by leukotrienes => ECO:0000269|PubMed:7667299 |
Chain | Residue | Details |
L | TYR378 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
L | LYS72 | |
L | LYS336 | |
L | LYS413 | |
L | LYS572 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:9395533 |
Chain | Residue | Details |
L | SER415 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1h19 |
Chain | Residue | Details |
L | TYR383 | |
L | GLU296 | |
L | GLU271 |
site_id | MCSA1 |
Number of Residues | 7 |
Details | M-CSA 166 |
Chain | Residue | Details |
L | GLU271 | electrostatic stabiliser, hydrogen bond acceptor, nucleofuge, nucleophile |
L | HIS295 | metal ligand |
L | GLU296 | electrostatic stabiliser |
L | HIS299 | metal ligand |
L | GLU318 | metal ligand |
L | ASP375 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
L | TYR383 | electrostatic stabiliser |