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3H7U

Crystal structure of the plant stress-response enzyme AKR4C9

Functional Information from GO Data
ChainGOidnamespacecontents
A0004033molecular_functionaldo-keto reductase (NADPH) activity
A0005783cellular_componentendoplasmic reticulum
A0008106molecular_functionalcohol dehydrogenase (NADP+) activity
A0009409biological_processresponse to cold
A0009414biological_processresponse to water deprivation
A0009507cellular_componentchloroplast
A0009636biological_processresponse to toxic substance
A0009651biological_processresponse to salt stress
A0016229molecular_functionsteroid dehydrogenase activity
A0016491molecular_functionoxidoreductase activity
A0070401molecular_functionNADP+ binding
Functional Information from PDB Data
site_idAC1
Number of Residues36
DetailsBINDING SITE FOR RESIDUE NAP A 401
ChainResidue
AGLY22
AGLN180
ATYR206
ASER207
APRO208
ALEU209
AGLY210
ASER211
APRO212
AGLY213
AALA239
ATHR23
ALEU254
APRO255
ALYS256
ASER257
ATHR258
AARG262
AGLU265
AASN266
AACT501
AHOH618
ATRP24
AHOH656
AHOH658
AHOH688
AHOH736
AHOH775
AHOH844
AHOH955
AASP47
ATYR52
AHIS114
ATRP115
ASER158
AASN159

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A 501
ChainResidue
ATRP24
ATYR52
AARG69
AHIS114
ATRP115
ANAP401

Functional Information from PROSITE/UniProt
site_idPS00062
Number of Residues18
DetailsALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. MealydsgkARAIGVSNF
ChainResidueDetails
AMET143-PHE160

site_idPS00063
Number of Residues16
DetailsALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. LPKSTNegRIkENfNV
ChainResidueDetails
ALEU254-VAL269

site_idPS00798
Number of Residues18
DetailsALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GYRHIDCAqiygnEkeIG
ChainResidueDetails
AGLY42-GLY59

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
ATYR52

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:19616008
ChainResidueDetails
ATHR23
AASP47
ASER158
AGLN180
ASER207
ALYS256
AARG262

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AHIS114

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:22223895
ChainResidueDetails
AALA2

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mrq
ChainResidueDetails
ALYS81
AASP47
AHIS114
ATYR52

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mrq
ChainResidueDetails
ALYS81
ATYR52

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PDB entries from 2024-10-30

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