Structure of PDB 2vhx Chain A

Receptor sequence
>2vhxA (length=368) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence]
MRVGIPTETKNNEFRVAITPAGVAELTRRGHEVLIQAGAGEGSAITDADF
KAAGAQLVGTADQVWADADLLLKVKEPIAAEYGRLRHGQILFTFLHLAAS
RACTDALLDSGTTSIAYETVQTADGALPLLAPMSEVAGRLAAQVGAYHLM
RTQGGRGVLMGGVPGVEPADVVVIGAGTAGYNAARIANGMGATVTVLDIN
IDKLRQLDAEFCGRIHTRYSSAYELEGAVKRADLVIGAVLVKAPKLVSNS
LVAHMKPGAVLVDIAIDQGGCFEGSRPTTYDHPTFAVHDTLFYCVANMPA
SVPKTSTYALTNATMPYVLELADHGWRAACRSNPALAKGLSTHEGALLSE
RVATDLGVPFTEPASVLA
3D structure
PDB2vhx Three-Dimensional Structures of Apo- and Holo-L-Alanine Dehydrogenase from Mycobacterium Tuberculosis Reveal Conformational Changes Upon Coenzyme Binding.
ChainA
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) R15 K75 F94 H96 E118 T122 P128 A131 D270
Catalytic site (residue number reindexed from 1) R15 K75 F94 H96 E118 T122 P128 A131 D267
Enzyme Commision number 1.4.1.1: alanine 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 PYR A R15 K75 F94 H96 M133 D270 N300 R15 K75 F94 H96 M133 D267 N297
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0000286 alanine dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
Biological Process
GO:0001666 response to hypoxia
GO:0006524 alanine catabolic process
GO:0042853 L-alanine catabolic process
Cellular Component
GO:0005576 extracellular region
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0009274 peptidoglycan-based cell wall

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2vhx, PDBe:2vhx, PDBj:2vhx
PDBsum2vhx
PubMed18304579
UniProtP9WQB1|DHA_MYCTU Alanine dehydrogenase (Gene Name=ald)

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