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3CKY

Structural and Kinetic Properties of a beta-hydroxyacid dehydrogenase involved in nicotinate fermentation

Functional Information from GO Data
ChainGOidnamespacecontents
A0016054biological_processorganic acid catabolic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0043718molecular_function2-hydroxymethylglutarate dehydrogenase activity
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
A1901848biological_processnicotinate catabolic process
B0016054biological_processorganic acid catabolic process
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0043718molecular_function2-hydroxymethylglutarate dehydrogenase activity
B0050661molecular_functionNADP binding
B0051287molecular_functionNAD binding
B1901848biological_processnicotinate catabolic process
C0016054biological_processorganic acid catabolic process
C0016491molecular_functionoxidoreductase activity
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0043718molecular_function2-hydroxymethylglutarate dehydrogenase activity
C0050661molecular_functionNADP binding
C0051287molecular_functionNAD binding
C1901848biological_processnicotinate catabolic process
D0016054biological_processorganic acid catabolic process
D0016491molecular_functionoxidoreductase activity
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0043718molecular_function2-hydroxymethylglutarate dehydrogenase activity
D0050661molecular_functionNADP binding
D0051287molecular_functionNAD binding
D1901848biological_processnicotinate catabolic process
Functional Information from PROSITE/UniProt
site_idPS00895
Number of Residues14
Details3_HYDROXYISOBUT_DH 3-hydroxyisobutyrate dehydrogenase signature. FIGLGaMGkpMAiN
ChainResidueDetails
APHE9-ASN22

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P0ABQ3
ChainResidueDetails
ALYS174
BLYS174
CLYS174
DLYS174

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P0ABQ3
ChainResidueDetails
AGLY8
DGLY8
DSER99
DLYS243
ASER99
ALYS243
BGLY8
BSER99
BLYS243
CGLY8
CSER99
CLYS243

227344

PDB entries from 2024-11-13

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