Structure of PDB 1nqt Chain I Binding Site BS01

Receptor Information
>1nqt Chain I (length=496) Species: 9913 (Bos taurus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DPNFFKMVEGFFDRGASIVEDKLVEDLRTRESEEQKRNRVRGILRIIKPC
NHVLSLSFPIRRDDGSWEVIEGYRAQHSHQRTPCKGGIRYSTDVSVDEVK
ALASLMTYKCAVVDVPFGGAKAGVKINPKNYTDNELEKITRRFTMELAKK
GFIGPGIDVPAPDMSTGEREMSWIADTYASTIGHYDINAHACVTGKPISQ
GGIHGRISATGRGVFHGIENFINEASYMSILGMTPGFGDKTFVVQGFGNV
GLHSMRYLHRFGAKCIAVGESDGSIWNPDGIDPKELEDFKLQHGSILGFP
KAKPYEGSILEADCDILIPAASEKQLTKSNAPRVKAKIIAEGANGPTTPE
ADKIFLERNIMVIPDLYLNAGGVTVSYFEWLKNLNHVSYGRLTFKYERDS
NYHLLMSVQESLERKFGKHGGTIPIVPTAEFQDRISGASEKDIVHSGLAY
TMERSARQIMRTAMKYNLGLDLRTAAYVNAIEKVFKVYNEAGVTFT
Ligand information
Ligand IDADP
InChIInChI=1S/C10H15N5O10P2/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(24-10)1-23-27(21,22)25-26(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKeyXTWYTFMLZFPYCI-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)OP(=O)(O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)O)O)O)N
FormulaC10 H15 N5 O10 P2
NameADENOSINE-5'-DIPHOSPHATE
ChEMBLCHEMBL14830
DrugBankDB16833
ZINCZINC000012360703
PDB chain1nqt Chain I Residue 502 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1nqt Structural studies on ADP activation of mammalian glutamate dehydrogenase and the evolution of regulation
Resolution3.5 Å
Binding residue
(original residue number in PDB)		Q85 R86 D119 V120 R459 K488 V489 V492
Binding residue
(residue number reindexed from 1)		Q80 R81 D114 V115 R454 K483 V484 V487
Annotation score3
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)(+)].
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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