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3EMK

2.5A crystal structure of glucose/ribitol dehydrogenase from brucella melitensis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004316molecular_function3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
A0006633biological_processfatty acid biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0051287molecular_functionNAD binding
B0004316molecular_function3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
B0006633biological_processfatty acid biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0051287molecular_functionNAD binding
C0004316molecular_function3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
C0006633biological_processfatty acid biosynthetic process
C0016491molecular_functionoxidoreductase activity
C0051287molecular_functionNAD binding
D0004316molecular_function3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
D0006633biological_processfatty acid biosynthetic process
D0016491molecular_functionoxidoreductase activity
D0051287molecular_functionNAD binding
Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. SivgvtgnpgQanYCASKAGLiGFSkSLA
ChainResidueDetails
ASER139-ALA167

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
AVAL143

site_idCSA10
Number of Residues4
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
BASN111
BTYR152
BLYS156
BSER139

site_idCSA11
Number of Residues4
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
CASN111
CTYR152
CLYS156
CSER139

site_idCSA12
Number of Residues4
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
DASN111
DTYR152
DLYS156
DSER139

site_idCSA13
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
ALYS156
AGLN149

site_idCSA14
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
BLYS156
BGLN149

site_idCSA15
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
CLYS156
CGLN149

site_idCSA16
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
DLYS156
DGLN149

site_idCSA17
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
ATYR152
ALYS156

site_idCSA18
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
BTYR152
BLYS156

site_idCSA19
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
CTYR152
CLYS156

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
BVAL143

site_idCSA20
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
DTYR152
DLYS156

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
CVAL143

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
DVAL143

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
ATYR152
ALYS156
ASER139

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
BTYR152
BLYS156
BSER139

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
CTYR152
CLYS156
CSER139

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
DTYR152
DLYS156
DSER139

site_idCSA9
Number of Residues4
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
AASN111
ATYR152
ALYS156
ASER139

223790

PDB entries from 2024-08-14

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