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3WYE

Crystal Structure of chimeric engineered (2S,3S)-butanediol dehydrogenase complexed with NAD+

Functional Information from GO Data
ChainGOidnamespacecontents
A0016491molecular_functionoxidoreductase activity
A0019152molecular_functionacetoin dehydrogenase (NAD+) activity
A0045150biological_processacetoin catabolic process
B0016491molecular_functionoxidoreductase activity
B0019152molecular_functionacetoin dehydrogenase (NAD+) activity
B0045150biological_processacetoin catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues27
DetailsBINDING SITE FOR RESIDUE NAD A 301
ChainResidue
AGLY9
AASN86
AALA138
ASER139
ATYR152
ALYS156
APRO182
AGLY183
AVAL185
ATHR187
AMET189
AGLN12
ATRP190
AHOH413
AHOH422
AHOH427
AHOH428
AHOH437
AHOH440
AHOH451
AGLY13
AILE14
AASP33
ATYR34
AVAL58
AASP59
AVAL60

site_idAC2
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NAD B 301
ChainResidue
BGLY9
BGLN12
BGLY13
BILE14
BASP33
BTYR34
BVAL58
BASP59
BVAL60
BASN86
BALA138
BSER139
BTYR152
BLYS156
BPRO182
BGLY183
BVAL185
BTHR187
BGLY188
BMET189
BTRP190
BHOH415
BHOH416
BHOH436

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. SiaaiqgfpiLsaYSTTKFAVrGLTqTAA
ChainResidueDetails
ASER139-ALA167

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:11173520
ChainResidueDetails
ALEU6
AASP59
BLEU6
BASP59

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:Q48436, ECO:0000255|PROSITE-ProRule:PRU10001
ChainResidueDetails
ATYR152
BTYR152

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:19941855
ChainResidueDetails
AASN86
ATYR152
ALYS156
APRO182
BASN86
BTYR152
BLYS156
BPRO182

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PDB entries from 2024-07-31

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