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1GEG

CRYATAL STRUCTURE ANALYSIS OF MESO-2,3-BUTANEDIOL DEHYDROGENASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0016491molecular_functionoxidoreductase activity
A0019152molecular_functionacetoin dehydrogenase (NAD+) activity
A0045150biological_processacetoin catabolic process
A0052588molecular_functiondiacetyl reductase ((S)-acetoin forming) (NAD+) activity
B0016491molecular_functionoxidoreductase activity
B0019152molecular_functionacetoin dehydrogenase (NAD+) activity
B0045150biological_processacetoin catabolic process
B0052588molecular_functiondiacetyl reductase ((S)-acetoin forming) (NAD+) activity
C0016491molecular_functionoxidoreductase activity
C0019152molecular_functionacetoin dehydrogenase (NAD+) activity
C0045150biological_processacetoin catabolic process
C0052588molecular_functiondiacetyl reductase ((S)-acetoin forming) (NAD+) activity
D0016491molecular_functionoxidoreductase activity
D0019152molecular_functionacetoin dehydrogenase (NAD+) activity
D0045150biological_processacetoin catabolic process
D0052588molecular_functiondiacetyl reductase ((S)-acetoin forming) (NAD+) activity
E0016491molecular_functionoxidoreductase activity
E0019152molecular_functionacetoin dehydrogenase (NAD+) activity
E0045150biological_processacetoin catabolic process
E0052588molecular_functiondiacetyl reductase ((S)-acetoin forming) (NAD+) activity
F0016491molecular_functionoxidoreductase activity
F0019152molecular_functionacetoin dehydrogenase (NAD+) activity
F0045150biological_processacetoin catabolic process
F0052588molecular_functiondiacetyl reductase ((S)-acetoin forming) (NAD+) activity
G0016491molecular_functionoxidoreductase activity
G0019152molecular_functionacetoin dehydrogenase (NAD+) activity
G0045150biological_processacetoin catabolic process
G0052588molecular_functiondiacetyl reductase ((S)-acetoin forming) (NAD+) activity
H0016491molecular_functionoxidoreductase activity
H0019152molecular_functionacetoin dehydrogenase (NAD+) activity
H0045150biological_processacetoin catabolic process
H0052588molecular_functiondiacetyl reductase ((S)-acetoin forming) (NAD+) activity
Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. SqaghvgnpeLavYSSSKFAVrGLTqTAA
ChainResidueDetails
ASER139-ALA167

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues232
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11173520","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
ATYR152
ALYS156
ASER139
AASN110

site_idCSA10
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
BLYS156
BLEU149

site_idCSA11
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
CLYS156
CLEU149

site_idCSA12
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
DLYS156
DLEU149

site_idCSA13
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
ELYS156
ELEU149

site_idCSA14
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
FLYS156
FLEU149

site_idCSA15
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
GLYS156
GLEU149

site_idCSA16
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
HLYS156
HLEU149

site_idCSA17
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
ATYR152
ALYS156

site_idCSA18
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
BTYR152
BLYS156

site_idCSA19
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
CTYR152
CLYS156

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
BTYR152
BLYS156
BSER139
BASN110

site_idCSA20
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
DTYR152
DLYS156

site_idCSA21
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
ETYR152
ELYS156

site_idCSA22
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
FTYR152
FLYS156

site_idCSA23
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
GTYR152
GLYS156

site_idCSA24
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
HTYR152
HLYS156

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
CTYR152
CLYS156
CSER139
CASN110

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
DTYR152
DLYS156
DSER139
DASN110

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
ETYR152
ELYS156
ESER139
EASN110

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
FTYR152
FLYS156
FSER139
FASN110

site_idCSA7
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
GTYR152
GLYS156
GSER139
GASN110

site_idCSA8
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
HTYR152
HLYS156
HSER139
HASN110

site_idCSA9
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
ALYS156
ALEU149

246704

PDB entries from 2025-12-24

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