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3F7J

B.subtilis YvgN

Replaces:  3B3E
Functional Information from GO Data
ChainGOidnamespacecontents
A0004033molecular_functionaldo-keto reductase (NADPH) activity
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0043892molecular_functionmethylglyoxal reductase (NADPH) activity
A0044281biological_processsmall molecule metabolic process
B0004033molecular_functionaldo-keto reductase (NADPH) activity
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0043892molecular_functionmethylglyoxal reductase (NADPH) activity
B0044281biological_processsmall molecule metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NO3 A 277
ChainResidue
APHE25
ASER190
APRO191
ALEU192
AMET193
AGLN194
APRO231
ALYS232

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NO3 A 278
ChainResidue
AGLY195
ALEU198
AALA215
AARG238
AHOH302
AHOH329
AHOH454
ALEU192

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 A 279
ChainResidue
AASP117
ALYS118
ATYR119
ALYS120
AASP121
AHOH570
AHOH666

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE NO3 A 280
ChainResidue
ATRP81
AASN82
ALEU274
APHE276
AHOH422
AHOH599
AHOH660
BTRP81
BLEU274
BK281

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NO3 A 281
ChainResidue
AASP177
ATYR178
AGLY181
AGLN182
AHOH577

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE NO3 B 277
ChainResidue
BPHE25
BSER190
BPRO191
BLEU192
BMET193
BGLN194
BPRO231
BLYS232
BHOH508

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE NO3 B 278
ChainResidue
BLEU192
BGLY195
BLEU198
BVAL214
BALA215
BARG238
BHOH295
BHOH301
BHOH395
BHOH467

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO3 B 279
ChainResidue
BASP117
BLYS118
BTYR119
BLYS120
BASP121
BHOH658

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NO3 B 280
ChainResidue
ALYS55
AHOH356
BALA52
BLYS55
BARG100
BHOH307
BHOH334
BHOH421

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE K B 281
ChainResidue
ANO3280
BTRP81
BASN82

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE K B 282
ChainResidue
AHOH486
BHOH668

Functional Information from PROSITE/UniProt
site_idPS00062
Number of Residues18
DetailsALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. LeklykdgkIRAIGVSNF
ChainResidueDetails
ALEU126-PHE143

site_idPS00063
Number of Residues16
DetailsALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. IPKSIKehRIiENaDI
ChainResidueDetails
AILE230-ILE245

site_idPS00798
Number of Residues18
DetailsALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GYRSIDTAaiyknEegVG
ChainResidueDetails
AGLY44-GLY61

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
ATYR54
BTYR54

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AHIS112
ASER190
BHIS112
BSER190

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mrq
ChainResidueDetails
ATYR54
ALYS79
AASP49
AHIS112

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mrq
ChainResidueDetails
BTYR54
BLYS79
BASP49
BHIS112

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mrq
ChainResidueDetails
ATYR54
ALYS79

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mrq
ChainResidueDetails
BTYR54
BLYS79

227344

PDB entries from 2024-11-13

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