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6KY6

Crystal structure of a thermostable aldo-keto reductase Tm1743 in complexs with inhibitor epalrestat in space group P3221cc

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0016491molecular_functionoxidoreductase activity
B0000166molecular_functionnucleotide binding
B0016491molecular_functionoxidoreductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues28
Detailsbinding site for residue NAP A 301
ChainResidue
AGLY19
ATYR198
ASER199
APRO200
ALEU201
AARG202
AARG203
ATHR204
ATYR226
AILE242
APRO243
ATHR20
ALYS244
AGLY246
AARG247
AHIS250
AGLU253
AASN254
AEPR302
AHOH437
AHOH439
ATRP21
AASP53
ATYR58
AHIS117
ASER147
AASN148
AGLN169

site_idAC2
Number of Residues5
Detailsbinding site for residue EPR A 302
ChainResidue
ATYR58
AHIS117
ANAP301
AHOH456
BCL303

site_idAC3
Number of Residues1
Detailsbinding site for residue CL A 303
ChainResidue
BEPR302

site_idAC4
Number of Residues4
Detailsbinding site for residue CL A 304
ChainResidue
ATYR49
APRO243
AALA245
AASN254

site_idAC5
Number of Residues27
Detailsbinding site for residue NAP B 301
ChainResidue
BGLY19
BTHR20
BTRP21
BASP53
BTYR58
BHIS117
BSER147
BASN148
BGLN169
BTYR198
BSER199
BPRO200
BLEU201
BARG203
BTHR204
BTYR226
BILE242
BPRO243
BLYS244
BGLY246
BARG247
BHIS250
BGLU253
BASN254
BEPR302
BHOH419
BHOH454

site_idAC6
Number of Residues5
Detailsbinding site for residue EPR B 302
ChainResidue
ACL303
BTYR58
BHIS117
BNAP301
BHOH497

site_idAC7
Number of Residues1
Detailsbinding site for residue CL B 303
ChainResidue
AEPR302

site_idAC8
Number of Residues2
Detailsbinding site for residue CL B 304
ChainResidue
BASN120
BHOH500

site_idAC9
Number of Residues1
Detailsbinding site for residue CL B 305
ChainResidue
BMET1

Functional Information from PROSITE/UniProt
site_idPS00062
Number of Residues18
DetailsALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. MaegvrqglIRYIGVSNF
ChainResidueDetails
AMET132-PHE149

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PDB entries from 2024-05-29

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