Structure of PDB 3etg Chain E

Receptor sequence
>3etgE (length=501) Species: 9913 (Bos taurus) [Search protein sequence]
ADREDDPNFFKMVEGFFDRGASIVEDKLVEDLKTRETEEQKRNRVRGILR
IIKPCNHVLSLSFPIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVS
VDEVKALASLMTYKCAVVDVPFGGAKAGVKINPKNYTDNELEKITRRFTM
ELAKKGFIGPGVDVPAPDMSTGEREMSWIADTYASTIGHYDINAHACVTG
KPISQGGIHGRISATGRGVFHGIENFINEASYMSILGMTPGFGDKTFAVQ
GFGNVGLHSMRYLHRFGAKCVAVGESDGSIWNPDGIDPKELEDFKLQHGT
ILGFPKAKIYEGSILEVDCDILIPAASEKQLTKSNAPRVKAKIIAEGANG
PTTPEADKIFLERNIMVIPDLYLNAGGVTVSYFEWLKNLNHVSYGRLTFK
YERDSNYHLLMSVQESLERKFGKHGGTIPIVPTAEFQDRISGASEKDIVH
SGLAYTMERSARQIMRTAMKYNLGLDLRTAAYVNAIEKVFRVYNEAGVTF
T
3D structure
PDB3etg Novel Inhibitors Complexed with Glutamate Dehydrogenase: ALLOSTERIC REGULATION BY CONTROL OF PROTEIN DYNAMICS
ChainE
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K126 D168
Catalytic site (residue number reindexed from 1) K126 D168
Enzyme Commision number 1.4.1.3: glutamate dehydrogenase [NAD(P)(+)].
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004352 glutamate dehydrogenase (NAD+) activity
GO:0004353 glutamate dehydrogenase [NAD(P)+] activity
GO:0004354 glutamate dehydrogenase (NADP+) activity
GO:0005524 ATP binding
GO:0005525 GTP binding
GO:0016491 oxidoreductase activity
GO:0016639 oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
GO:0042802 identical protein binding
Biological Process
GO:0006520 amino acid metabolic process
GO:0006538 glutamate catabolic process
GO:0006541 glutamine metabolic process
GO:0072350 tricarboxylic acid metabolic process
Cellular Component
GO:0005739 mitochondrion
GO:0005743 mitochondrial inner membrane
GO:0005783 endoplasmic reticulum

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3etg, PDBe:3etg, PDBj:3etg
PDBsum3etg
PubMed19531491
UniProtP00366|DHE3_BOVIN Glutamate dehydrogenase 1, mitochondrial (Gene Name=GLUD1)

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