5FWQ
Apo structure of human Leukotriene A4 hydrolase
Functional Information from GO Data
| Chain | GOid | namespace | contents | 
| A | 0003723 | molecular_function | RNA binding | 
| A | 0004177 | molecular_function | aminopeptidase activity | 
| A | 0004301 | molecular_function | epoxide hydrolase activity | 
| A | 0004463 | molecular_function | leukotriene-A4 hydrolase activity | 
| A | 0005515 | molecular_function | protein binding | 
| A | 0005576 | cellular_component | extracellular region | 
| A | 0005634 | cellular_component | nucleus | 
| A | 0005654 | cellular_component | nucleoplasm | 
| A | 0005737 | cellular_component | cytoplasm | 
| A | 0005829 | cellular_component | cytosol | 
| A | 0006508 | biological_process | proteolysis | 
| A | 0006629 | biological_process | lipid metabolic process | 
| A | 0006691 | biological_process | leukotriene metabolic process | 
| A | 0008233 | molecular_function | peptidase activity | 
| A | 0008237 | molecular_function | metallopeptidase activity | 
| A | 0008270 | molecular_function | zinc ion binding | 
| A | 0010043 | biological_process | response to zinc ion | 
| A | 0016787 | molecular_function | hydrolase activity | 
| A | 0019370 | biological_process | leukotriene biosynthetic process | 
| A | 0043171 | biological_process | peptide catabolic process | 
| A | 0043434 | biological_process | response to peptide hormone | 
| A | 0045148 | molecular_function | tripeptide aminopeptidase activity | 
| A | 0046872 | molecular_function | metal ion binding | 
| A | 0060509 | biological_process | type I pneumocyte differentiation | 
| A | 0070006 | molecular_function | metalloaminopeptidase activity | 
| A | 0070062 | cellular_component | extracellular exosome | 
| A | 1904724 | cellular_component | tertiary granule lumen | 
| A | 1904813 | cellular_component | ficolin-1-rich granule lumen | 
Functional Information from PDB Data
| site_id | AC1 | 
| Number of Residues | 4 | 
| Details | BINDING SITE FOR RESIDUE YB A 2612 | 
| Chain | Residue | 
| A | GLU46 | 
| A | ASP175 | 
| A | HOH2031 | 
| A | HOH2032 | 
| site_id | AC2 | 
| Number of Residues | 9 | 
| Details | BINDING SITE FOR RESIDUE ACT A 1611 | 
| Chain | Residue | 
| A | GLU318 | 
| A | TYR383 | 
| A | ZN1612 | 
| A | HOH2114 | 
| A | GLY269 | 
| A | GLU271 | 
| A | HIS295 | 
| A | GLU296 | 
| A | HIS299 | 
| site_id | AC3 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE ZN A 1612 | 
| Chain | Residue | 
| A | HIS295 | 
| A | HIS299 | 
| A | GLU318 | 
| A | TYR383 | 
| A | ACT1611 | 
| site_id | AC4 | 
| Number of Residues | 7 | 
| Details | BINDING SITE FOR RESIDUE YB A 1613 | 
| Chain | Residue | 
| A | ASP47 | 
| A | ASP481 | 
| A | HOH2036 | 
| A | HOH2330 | 
| A | HOH2331 | 
| A | HOH2406 | 
| A | HOH2407 | 
| site_id | AC5 | 
| Number of Residues | 2 | 
| Details | BINDING SITE FOR RESIDUE YB A 1614 | 
| Chain | Residue | 
| A | GLU70 | 
| A | GLU121 | 
| site_id | AC6 | 
| Number of Residues | 3 | 
| Details | BINDING SITE FOR RESIDUE YB A 1615 | 
| Chain | Residue | 
| A | ASP422 | 
| A | ASP426 | 
| A | HOH2294 | 
| site_id | AC7 | 
| Number of Residues | 7 | 
| Details | BINDING SITE FOR RESIDUE YB A 1616 | 
| Chain | Residue | 
| A | ASP47 | 
| A | ASP481 | 
| A | HOH2036 | 
| A | HOH2330 | 
| A | HOH2331 | 
| A | HOH2406 | 
| A | HOH2407 | 
| site_id | AC8 | 
| Number of Residues | 3 | 
| Details | BINDING SITE FOR RESIDUE YB A 1617 | 
| Chain | Residue | 
| A | GLU46 | 
| A | ASP175 | 
| A | HOH2032 | 
| site_id | AC9 | 
| Number of Residues | 6 | 
| Details | BINDING SITE FOR RESIDUE IMD A 1618 | 
| Chain | Residue | 
| A | GLN136 | 
| A | TYR267 | 
| A | PHE314 | 
| A | PRO374 | 
| A | ASP375 | 
| A | HOH2265 | 
| site_id | BC1 | 
| Number of Residues | 4 | 
| Details | BINDING SITE FOR RESIDUE IMD A 1619 | 
| Chain | Residue | 
| A | TRP311 | 
| A | PHE314 | 
| A | ALA377 | 
| A | HOH2265 | 
| site_id | BC2 | 
| Number of Residues | 6 | 
| Details | BINDING SITE FOR RESIDUE IMD A 1620 | 
| Chain | Residue | 
| A | GLY344 | 
| A | GLY347 | 
| A | GLU348 | 
| A | GLU501 | 
| A | ALA504 | 
| A | GLN508 | 
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 | VAL292-TRP301 | 
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 | 
| Number of Residues | 1 | 
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"11675384","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12207002","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"24591641","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1H19","evidenceCode":"ECO:0007744"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI2 | 
| Number of Residues | 1 | 
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"11675384","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12207002","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"24591641","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1H19","evidenceCode":"ECO:0007744"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI3 | 
| Number of Residues | 9 | 
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18804029","evidenceCode":"ECO:0000269"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI4 | 
| Number of Residues | 2 | 
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11175901","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11675384","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11917124","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12207002","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15078870","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18804029","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19618939","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24591641","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GW6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1H19","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1HS6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2R59","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2VJ8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3B7R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3B7S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3B7T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3B7U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CHO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CHP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CHQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CHR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CHS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FH5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FH7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FH8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FHE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FTS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FTU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FTV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FTW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FTX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FTY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FTZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FU0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FU3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FU5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FU6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FUD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FUE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FUF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FUH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FUI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FUJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FUK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FUL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FUM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FUN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3U9W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4DPR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4L2L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4MKT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4MS6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5AEN","evidenceCode":"ECO:0007744"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI5 | 
| Number of Residues | 1 | 
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11175901","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24591641","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GW6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1H19","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1HS6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2R59","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2VJ8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3B7R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3B7S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3B7T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3B7U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CHO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CHP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CHQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CHR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CHS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FH5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FH7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FH8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FHE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FTS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FTU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FTV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FTW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FTX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FTY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FTZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FU0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FU3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FU5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FU6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FUD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FUE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FUF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FUH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FUI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FUJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FUK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FUL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FUM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FUN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3U9W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4DPR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4L2L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4MKT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4MS6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5AEN","evidenceCode":"ECO:0007744"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI6 | 
| Number of Residues | 2 | 
| Details | Site: {"description":"Pro-Gly-Pro binding","evidences":[{"source":"PubMed","id":"24591641","evidenceCode":"ECO:0000269"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI7 | 
| Number of Residues | 1 | 
| Details | Site: {"description":"Essential for epoxide hydrolase activity, but not for aminopeptidase activity","evidences":[{"source":"PubMed","id":"11917124","evidenceCode":"ECO:0000269"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI8 | 
| Number of Residues | 1 | 
| Details | Site: {"description":"Covalently modified during suicide inhibition by leukotrienes","evidences":[{"source":"PubMed","id":"7667299","evidenceCode":"ECO:0000269"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI9 | 
| Number of Residues | 4 | 
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI10 | 
| Number of Residues | 1 | 
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"9395533","evidenceCode":"ECO:0000269"}]} | 
| Chain | Residue | Details | 
Catalytic Information from CSA
| site_id | MCSA1 | 
| Number of Residues | 7 | 
| Details | M-CSA 166 | 
| Chain | Residue | Details | 
| A | GLU271 | electrostatic stabiliser, hydrogen bond acceptor, nucleofuge, nucleophile | 
| A | HIS295 | metal ligand | 
| A | GLU296 | electrostatic stabiliser | 
| A | HIS299 | metal ligand | 
| A | GLU318 | metal ligand | 
| A | ASP375 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor | 
| A | TYR383 | electrostatic stabiliser | 






