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1V3U

Crystal structure of leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase in apo form

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006693biological_processprostaglandin metabolic process
A0016491molecular_functionoxidoreductase activity
A0016628molecular_functionoxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor
A0032440molecular_function2-alkenal reductase [NAD(P)H] activity
A0035798molecular_function2-alkenal reductase (NADPH) activity
A0036102biological_processleukotriene B4 metabolic process
A0036185molecular_function13-lipoxin reductase activity
A0047522molecular_function15-oxoprostaglandin 13-reductase [NAD(P)+] activity
A0097257molecular_functionleukotriene B4 12-hydroxy dehydrogenase activity
A2001302biological_processlipoxin A4 metabolic process
B0005737cellular_componentcytoplasm
B0006629biological_processlipid metabolic process
B0006631biological_processfatty acid metabolic process
B0006693biological_processprostaglandin metabolic process
B0016491molecular_functionoxidoreductase activity
B0016628molecular_functionoxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor
B0032440molecular_function2-alkenal reductase [NAD(P)H] activity
B0035798molecular_function2-alkenal reductase (NADPH) activity
B0036102biological_processleukotriene B4 metabolic process
B0036185molecular_function13-lipoxin reductase activity
B0047522molecular_function15-oxoprostaglandin 13-reductase [NAD(P)+] activity
B0097257molecular_functionleukotriene B4 12-hydroxy dehydrogenase activity
B2001302biological_processlipoxin A4 metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1001
ChainResidue
ALYS324
AALA325
AHOH1045

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CL B 1002
ChainResidue
BHOH1119
BALA149
BALA151
BALA173
BGLY174
BLYS178
BHOH1106

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B 1003
ChainResidue
BHIS12
BPHE13
BSER54
BLYS55
BHOH1126

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 1004
ChainResidue
AARG70
AVAL72

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 1005
ChainResidue
BASN321
BLYS324
BALA325
BHOH1027

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 1006
ChainResidue
AALA149
AALA151
AALA173
ALYS178
AHOH1257

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 1007
ChainResidue
BHIS12
BGLU59

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15007077","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q14914","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q14914","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q91YR9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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