Structure of PDB 1bgv Chain A

Receptor sequence
>1bgvA (length=449) Species: 1512 ([Clostridium] symbiosum) [Search protein sequence]
SKYVDRVIAEVEKKYADEPEFVQTVEEVLSSLGPVVDAHPEYEEVALLER
MVIPERVIEFRVPWEDDNGKVHVNTGYRVQFNGAIGPYKGGLRFAPSVNL
SIMKFLGFEQAFKDSLTTLPMGGAKGGSDFDPNGKSDREVMRFCQAFMTE
LYRHIGPDIDVPAGDLGVGAREIGYMYGQYRKIVGGFYNGVLTGKARSFG
GSLVRPEATGYGSVYYVEAVMKHENDTLVGKTVALAGFGNVAWGAAKKLA
ELGAKAVTLSGPDGYIYDPEGITTEEKINYMLEMRASGRNKVQDYADKFG
VQFFPGEKPWGQKVDIIMPCATQNDVDLEQAKKIVANNVKYYIEVANMPT
TNEALRFLMQQPNMVVAPSKAVNAGGVLVSGFEMSQNSERLSWTAEEVDS
KLHQVMTDIHDGSAAAAERYGLGYNLVAGANIVGFQKIADAMMAQGIAW
3D structure
PDB1bgv Conformational flexibility in glutamate dehydrogenase. Role of water in substrate recognition and catalysis.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K125 D165
Catalytic site (residue number reindexed from 1) K125 D165
Enzyme Commision number 1.4.1.2: glutamate 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 GLU A K89 K113 A163 S380 K89 K113 A163 S380
Gene Ontology
Molecular Function
GO:0004352 glutamate dehydrogenase (NAD+) activity
GO:0004353 glutamate dehydrogenase [NAD(P)+] activity
GO:0004354 glutamate dehydrogenase (NADP+) 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:0006537 glutamate biosynthetic process
GO:0019552 glutamate catabolic process via 2-hydroxyglutarate
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1bgv, PDBe:1bgv, PDBj:1bgv
PDBsum1bgv
PubMed8263917
UniProtP24295|DHE2_CLOSY NAD-specific glutamate dehydrogenase (Gene Name=gdh)

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