Structure of PDB 1nqt Chain J

Receptor sequence
>1nqtJ (length=496) Species: 9913 (Bos taurus) [Search protein sequence]
DPNFFKMVEGFFDRGASIVEDKLVEDLRTRESEEQKRNRVRGILRIIKPC
NHVLSLSFPIRRDDGSWEVIEGYRAQHSHQRTPCKGGIRYSTDVSVDEVK
ALASLMTYKCAVVDVPFGGAKAGVKINPKNYTDNELEKITRRFTMELAKK
GFIGPGIDVPAPDMSTGEREMSWIADTYASTIGHYDINAHACVTGKPISQ
GGIHGRISATGRGVFHGIENFINEASYMSILGMTPGFGDKTFVVQGFGNV
GLHSMRYLHRFGAKCIAVGESDGSIWNPDGIDPKELEDFKLQHGSILGFP
KAKPYEGSILEADCDILIPAASEKQLTKSNAPRVKAKIIAEGANGPTTPE
ADKIFLERNIMVIPDLYLNAGGVTVSYFEWLKNLNHVSYGRLTFKYERDS
NYHLLMSVQESLERKFGKHGGTIPIVPTAEFQDRISGASEKDIVHSGLAY
TMERSARQIMRTAMKYNLGLDLRTAAYVNAIEKVFKVYNEAGVTFT
3D structure
PDB1nqt Structural studies on ADP activation of mammalian glutamate dehydrogenase and the evolution of regulation
ChainJ
Resolution3.5 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) K121 D163
Enzyme Commision number 1.4.1.3: glutamate dehydrogenase [NAD(P)(+)].
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 ADP J I203 H209 S393 R396 I198 H204 S388 R391
BS02 ADP J Q85 R86 A116 D119 V120 R459 K488 V489 Q80 R81 A111 D114 V115 R454 K483 V484
Gene Ontology
Molecular Function
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

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Molecular Function
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Biological Process
External links
PDB RCSB:1nqt, PDBe:1nqt, PDBj:1nqt
PDBsum1nqt
PubMed12653548
UniProtP00366|DHE3_BOVIN Glutamate dehydrogenase 1, mitochondrial (Gene Name=GLUD1)

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