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3H7R

Crystal structure of the plant stress-response enzyme AKR4C8

Functional Information from GO Data
ChainGOidnamespacecontents
A0004033molecular_functionaldo-keto reductase (NADPH) activity
A0005783cellular_componentendoplasmic reticulum
A0005829cellular_componentcytosol
A0009409biological_processresponse to cold
A0009414biological_processresponse to water deprivation
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 Residues33
DetailsBINDING SITE FOR RESIDUE NAP A 401
ChainResidue
AGLY22
ATYR202
ASER203
APRO204
ALEU205
AGLY206
ASER207
AGLN208
AARG214
AALA235
ALEU250
ATHR23
APRO251
ALYS252
ASER253
ASER254
AARG258
AGLU261
AASN262
AACT501
AHOH637
AHOH836
ATYR24
AHOH839
AHOH972
AHOH993
AHOH1002
AASP43
ATYR48
AHIS110
ASER154
AASN155
AGLN176

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A 501
ChainResidue
ATYR24
ATYR48
AHIS110
ANAP401
AHOH692
AHOH951

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 502
ChainResidue
APRO17
ACYS18
AVAL19
AARG40
AHIS41
AHOH787

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 503
ChainResidue
AGLN185
AGLY187
ALEU188
AGLU310
AHOH652
AHOH710

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 504
ChainResidue
ATHR123
APRO124
ATHR290
AGLU291
AALA293
AHIS294
AHOH747
AHOH997

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 505
ChainResidue
ALYS15
ALEU72
APHE73
AHOH633
AHOH739
AHOH926

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE EDO A 506
ChainResidue
AILE35
ALYS36
AILE37
AILE37
AGLY38
AARG40
APHE66
AHOH734
AHOH768
AHOH948

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 507
ChainResidue
AALA141
ALYS216
AEDO508
AHOH845
AHOH920
AHOH953

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 508
ChainResidue
AGLU140
AALA141
AASP144
AARG169
ALYS216
AEDO507
AHOH676
AHOH766
AHOH958

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 509
ChainResidue
AGLU9
AASN11
ALYS52
AGLY196
AHOH703

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 510
ChainResidue
AHOH974
AGLU125
AGLU284
AARG288
AHOH905

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 511
ChainResidue
ALEU127
AHIS297
APHE299

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 512
ChainResidue
AGLN184
AGLN186
AGLN283
AHOH621
AHOH765
AHOH813

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 513
ChainResidue
AGLU291
APHE292
AHOH692
AHOH723

Functional Information from PROSITE/UniProt
site_idPS00062
Number of Residues18
DetailsALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. MealydsgkARAIGVSNF
ChainResidueDetails
AMET139-PHE156

site_idPS00063
Number of Residues16
DetailsALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. LPKSSSgaRLkENlDV
ChainResidueDetails
ALEU250-VAL265

site_idPS00798
Number of Residues18
DetailsALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GYRHIDCAsiygnEkeIG
ChainResidueDetails
AGLY38-GLY55

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
ATYR48

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:19616008
ChainResidueDetails
ATHR23
AASP43
AHIS110
ASER154
AGLN176
ASER203
ALYS252
AARG258

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:Q0PGJ6
ChainResidueDetails
AALA2

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mrq
ChainResidueDetails
ATYR48
AASP43
AHIS110
ALYS77

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mrq
ChainResidueDetails
ATYR48
ALYS77

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PDB entries from 2024-07-10

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