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1V3T

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
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
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 Residues34
DetailsBINDING SITE FOR RESIDUE NAP A 1350
ChainResidue
APRO48
ATYR193
AASN217
AVAL218
ACYS239
AGLY240
AILE242
ASER243
ATYR245
APHE270
AILE271
AMET124
AVAL272
AMET316
ALEU317
AGLY319
AASN321
AHOH1352
AHOH1355
AHOH1357
AHOH1362
AHOH1421
ATHR128
AHOH1452
AHOH1468
AHOH1473
AHOH1502
AHOH1728
AGLY152
AALA153
AVAL154
AALA173
AGLY174
ALYS178

site_idAC2
Number of Residues37
DetailsBINDING SITE FOR RESIDUE NAP B 2350
ChainResidue
BPRO48
BMET124
BTHR128
BGLY152
BALA153
BVAL154
BALA173
BGLY174
BLYS178
BTYR193
BASN217
BVAL218
BCYS239
BGLY240
BALA241
BILE242
BTYR245
BPHE270
BILE271
BVAL272
BMET316
BLEU317
BGLY319
BASN321
BHOH2356
BHOH2362
BHOH2367
BHOH2379
BHOH2504
BHOH2533
BHOH2534
BHOH2542
BHOH2559
BHOH2648
BHOH2724
BHOH2728
BHOH2765

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

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PDB entries from 2024-07-10

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