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4GAA

Structure of Leukotriene A4 hydrolase from Xenopus laevis complexed with inhibitor bestatin

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0004301molecular_functionepoxide hydrolase activity
A0004463molecular_functionleukotriene-A4 hydrolase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0016787molecular_functionhydrolase activity
A0019370biological_processleukotriene biosynthetic process
A0043171biological_processpeptide catabolic process
A0045148molecular_functiontripeptide aminopeptidase activity
A0046872molecular_functionmetal ion binding
A0070006molecular_functionmetalloaminopeptidase activity
B0004177molecular_functionaminopeptidase activity
B0004301molecular_functionepoxide hydrolase activity
B0004463molecular_functionleukotriene-A4 hydrolase activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
B0016787molecular_functionhydrolase activity
B0019370biological_processleukotriene biosynthetic process
B0043171biological_processpeptide catabolic process
B0045148molecular_functiontripeptide aminopeptidase activity
B0046872molecular_functionmetal ion binding
B0070006molecular_functionmetalloaminopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 701
ChainResidue
AHIS292
AHIS296
AGLU315
ABES702

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE BES A 702
ChainResidue
AGLU268
AHIS292
AGLU293
AHIS296
AGLU315
APHE375
ATYR380
AARG560
AZN701
AHOH836
AGLN133
ATYR264
AGLY265
AGLY266
AMET267

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 701
ChainResidue
BHIS292
BHIS296
BGLU315
BBES702

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE BES B 702
ChainResidue
BGLN131
BGLN133
BTYR264
BGLY265
BGLY266
BGLU268
BHIS292
BGLU293
BHIS296
BGLU315
BPHE375
BTYR380
BARG560
BZN701

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VIAHEISHSW
ChainResidueDetails
AVAL289-TRP298

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PIRSR","id":"PIRSR634015-1","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PIRSR","id":"PIRSR634015-1","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P09960","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PIRSR","id":"PIRSR634015-3","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24333438","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4GAA","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsSite: {"description":"Pro-Gly-Pro binding","evidences":[{"source":"UniProtKB","id":"P09960","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsSite: {"description":"Essential for epoxide hydrolase activity, but not for aminopeptidase activity","evidences":[{"source":"UniProtKB","id":"P09960","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

250835

PDB entries from 2026-03-18

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