Structure of PDB 1geg Chain H

Receptor sequence
>1gegH (length=255) Species: 573 (Klebsiella pneumoniae) [Search protein sequence]
KKVALVTGAGQGIGKAIALRLVKDGFAVAIADYNDATAKAVASEINQAGG
HAVAVKVDVSDRDQVFAAVEQARKTLGGFDVIVNNAGVAPSTPIESITPE
IVDKVYNINVKGVIWGIQAAVEAFKKEGHGGKIINACSQAGHVGNPELAV
YSSSKFAVRGLTQTAARDLAPLGITVNGYCPGIVKTPMWAEIDRQVSEAA
GKPLGYGTAEFAKRITLGRLSEPEDVAACVSYLASPDSDYMTGQSLLIDG
GMVFN
3D structure
PDB1geg Crystal structure of meso-2,3-butanediol dehydrogenase in a complex with NAD+ and inhibitor mercaptoethanol at 1.7 A resolution for understanding of chiral substrate recognition mechanisms.
ChainH
Resolution1.7 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 S139 Y152 K156 V197
Catalytic site (residue number reindexed from 1) G12 S138 Y151 K155 V196
Enzyme Commision number 1.1.1.304: diacetyl reductase [(S)-acetoin forming].
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 GLC H R63 D64 F67 R62 D63 F66
BS02 NAD H G9 Q12 I14 D33 Y34 V58 D59 V60 N86 A87 I109 S139 Y152 K156 P182 V185 T187 M189 G8 Q11 I13 D32 Y33 V57 D58 V59 N85 A86 I108 S138 Y151 K155 P181 V184 T186 M188
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0019152 acetoin dehydrogenase (NAD+) activity
GO:0052588 diacetyl reductase ((S)-acetoin forming) (NAD+) activity
Biological Process
GO:0045150 acetoin catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1geg, PDBe:1geg, PDBj:1geg
PDBsum1geg
PubMed11173520
UniProtQ48436|BUDC_KLEPN Diacetyl reductase [(S)-acetoin forming] (Gene Name=budC)

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