Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3O3R

Crystal Structure of AKR1B14 in complex with NADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004032molecular_functionaldose reductase (NADPH) activity
A0004033molecular_functionaldo-keto reductase (NADPH) activity
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006693biological_processprostaglandin metabolic process
A0016491molecular_functionoxidoreductase activity
A0036130molecular_functionprostaglandin H2 endoperoxidase reductase activity
B0004032molecular_functionaldose reductase (NADPH) activity
B0004033molecular_functionaldo-keto reductase (NADPH) activity
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0006693biological_processprostaglandin metabolic process
B0016491molecular_functionoxidoreductase activity
B0036130molecular_functionprostaglandin H2 endoperoxidase reductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues31
DetailsBINDING SITE FOR RESIDUE NAP A 317
ChainResidue
AGLY19
ATYR210
ASER211
APRO212
ALEU213
AGLY214
ASER215
APRO216
AASP217
AALA246
AILE261
ATHR20
APRO262
ALYS263
ASER264
AVAL265
ATHR266
AHIS269
AGLU272
AASN273
AHOH430
AHOH442
ATRP21
AHOH474
AHOH504
AASP44
ATYR49
AHIS111
ASER160
AASN161
AGLN184

site_idAC2
Number of Residues34
DetailsBINDING SITE FOR RESIDUE NAP B 317
ChainResidue
BGLY19
BTHR20
BTRP21
BLYS22
BASP44
BTYR49
BHIS111
BSER160
BASN161
BGLN184
BTYR210
BSER211
BPRO212
BLEU213
BGLY214
BSER215
BPRO216
BASP217
BALA246
BILE261
BPRO262
BLYS263
BSER264
BVAL265
BTHR266
BHIS269
BGLU272
BASN273
BHOH450
BHOH459
BHOH468
BHOH531
BHOH570
BHOH577

Functional Information from PROSITE/UniProt
site_idPS00062
Number of Residues18
DetailsALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. MeelvdqglVKALGVSNF
ChainResidueDetails
AMET145-PHE162

site_idPS00798
Number of Residues18
DetailsALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GYRHFDCAyvyqnEseVG
ChainResidueDetails
AGLY39-GLY56

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
ATYR49
BTYR49

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:21168333
ChainResidueDetails
ATHR20
BSER160
BGLN184
BTYR210
BLYS263
BASN273
AASP44
ASER160
AGLN184
ATYR210
ALYS263
AASN273
BTHR20
BASP44

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Lowers pKa of active site Tyr => ECO:0000250
ChainResidueDetails
ALYS78
BLYS78

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon