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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)+] activity
A0035798molecular_function2-alkenal reductase (NADPH) activity
A0036102biological_processleukotriene B4 metabolic process
A0036132molecular_function13-prostaglandin reductase activity
A0036185molecular_function13-lipoxin reductase activity
A0047522molecular_function15-oxoprostaglandin 13-oxidase 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)+] activity
B0035798molecular_function2-alkenal reductase (NADPH) activity
B0036102biological_processleukotriene B4 metabolic process
B0036132molecular_function13-prostaglandin reductase activity
B0036185molecular_function13-lipoxin reductase activity
B0047522molecular_function15-oxoprostaglandin 13-oxidase 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 Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:15007077
ChainResidueDetails
AGLY152
BTYR193
BASN217
BCYS239
BPHE270
BASN321
ALYS178
ATYR193
AASN217
ACYS239
APHE270
AASN321
BGLY152
BLYS178

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q14914
ChainResidueDetails
ATHR18
BTHR18

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q14914
ChainResidueDetails
ASER20
BSER20

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:Q91YR9
ChainResidueDetails
ALYS178
BLYS178

218853

건을2024-04-24부터공개중

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