Structure of PDB 4xgi Chain D Binding Site BS02

Receptor Information
>4xgi Chain D (length=415) Species: 271848 (Burkholderia thailandensis E264) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SIPSYLHADDLGPWGNYLQQVDRVAPYLGSLSRWIETLKRPKRILIVDVP
IELDNGTVAHFEGYRVQHNVSRGPGKGGVRYHQDVTLSEVMALSAWMSVK
NAAVNVPYGGAKGGIRVDPRKLSRGELERVTRRYTSEIGIIIGPNTDIPA
PDVNTNEQIMAWMMDTYSMNQGQTATGVVTGKPISLGGSLGRKEATGRGV
FVVGCEAAKKKGVEIEGARIAVQGFGNVGGIAAKLFQEAGAKVIAVQDHT
GTIHQPAGVDTAKLLDHVGRTGGVAGFEGAEPMPNDEFWTVETEILIPAA
LENQITEKNASKIRTKIIVEGANGPTTTAADDILSANGVLVIPDVIANAG
GVTVSYFEWVQTEDEINHRLERVMREAFAGVWAVAEEHKVSVRTAAFIVA
CKRILMAREMRGLYP
Ligand information
Ligand IDAKG
InChIInChI=1S/C5H6O5/c6-3(5(9)10)1-2-4(7)8/h1-2H2,(H,7,8)(H,9,10)
InChIKeyKPGXRSRHYNQIFN-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=C(O)C(=O)CCC(=O)O
OpenEye OEToolkits 1.7.6C(CC(=O)O)C(=O)C(=O)O
CACTVS 3.385OC(=O)CCC(=O)C(O)=O
FormulaC5 H6 O5
Name2-OXOGLUTARIC ACID
ChEMBLCHEMBL1686
DrugBankDB08845
ZINCZINC000001532519
PDB chain4xgi Chain D Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4xgi Crystal structure of Glutamate dehydrogenase from Burkholderia thailandensis
Resolution2.0 Å
Binding residue
(original residue number in PDB)
K88 G89 G90 M109 K112 K124 A162 R204 G363 S367
Binding residue
(residue number reindexed from 1)
K76 G77 G78 M97 K100 K112 A150 R192 G351 S355
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) K124 D164
Catalytic site (residue number reindexed from 1) K112 D152
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004352 glutamate dehydrogenase (NAD+) activity
GO:0004353 glutamate dehydrogenase [NAD(P)+] activity
GO:0016491 oxidoreductase activity
GO:0016639 oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
Biological Process
GO:0006520 amino acid metabolic process
GO:0006538 glutamate catabolic process

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Molecular Function

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Biological Process
External links
PDB RCSB:4xgi, PDBe:4xgi, PDBj:4xgi
PDBsum4xgi
PubMed
UniProtQ2SZ78

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