Structure of PDB 3a28 Chain H

Receptor sequence
>3a28H (length=257) Species: 1718 (Corynebacterium glutamicum) [Search protein sequence]
SKVAMVTGGAQGIGRGISEKLAADGFDIAVADLPQQEEQAAETIKLIEAA
DQKAVFVGLDVTDKANFDSAIDEAAEKLGGFDVLVNNAGIAQIKPLLEVT
EEDLKQIYSVNVFSVFFGIQAASRKFDELGVKGKIINAASIAAIQGFPIL
SAYSTTKFAVRGLTQAAAQELAPKGHTVNAYAPGIVGTGMWEQIDAELSK
INGKPIGENFKEYSSSIALGRPSVPEDVAGLVSFLASENSNYVTGQVMLV
DGGMLYN
3D structure
PDB3a28 Structural basis for chiral substrate recognition by two 2,3-butanediol dehydrogenases
ChainH
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G13 S141 Y154 K158 L199
Catalytic site (residue number reindexed from 1) G12 S140 Y153 K157 L198
Enzyme Commision number 1.1.1.304: diacetyl reductase [(S)-acetoin forming].
1.1.1.76: (S,S)-butanediol dehydrogenase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 NAD H G9 Q12 G13 I14 D33 Q37 L60 D61 V62 N88 A89 S141 Y154 K158 P184 V187 T189 M191 G8 Q11 G12 I13 D32 Q36 L59 D60 V61 N87 A88 S140 Y153 K157 P183 V186 T188 M190
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0019152 acetoin dehydrogenase (NAD+) activity
GO:0047512 (S,S)-butanediol dehydrogenase activity
GO:0052588 diacetyl reductase ((S)-acetoin forming) (NAD+) activity
GO:0070403 NAD+ binding
GO:0070404 NADH binding
Biological Process
GO:0034077 butanediol metabolic process
GO:0045149 acetoin metabolic process
GO:0045150 acetoin catabolic process
GO:0051289 protein homotetramerization

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Molecular Function
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Biological Process
External links
PDB RCSB:3a28, PDBe:3a28, PDBj:3a28
PDBsum3a28
PubMed19941855
UniProtQ9ZNN8|BUDC_CORGT L-2,3-butanediol dehydrogenase (Gene Name=budC)

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