Structure of PDB 6dhd Chain B Binding Site BS02

Receptor Information
>6dhd Chain B (length=501) Species: 9913 (Bos taurus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ADREDDPNFFKMVEGFFDRGASIVEDKLVEDLKTRETEEQKRNRVRGILR
IIKPCNHVLSLSFPIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVS
VDEVKALASLMTYKCAVVDVPFGGAKAGVKINPKNYTDNELEKITRRFTM
ELAKKGFIGPGVDVPAPDMSTGEREMSWIADTYASTIGHYDINAHACVTG
KPISQGGIHGRISATGRGVFHGIENFINEASYMSILGMTPGFGDKTFAVQ
GFGNVGLHSMRYLHRFGAKCVAVGESDGSIWNPDGIDPKELEDFKLQHGT
ILGFPKAKIYEGSILEVDCDILIPAASEKQLTKSNAPRVKAKIIAEGANG
PTTPEADKIFLERNIMVIPDLYLNAGGVTVSYFEWLKNLNHVSYGRLTFK
YERDSNYHLLMSVQESLERKFGKHGGTIPIVPTAEFQDRISGASEKDIVH
SGLAYTMERSARQIMRTAMKYNLGLDLRTAAYVNAIEKVFRVYNEAGVTF
T
Ligand information
Ligand IDGLU
InChIInChI=1S/C5H9NO4/c6-3(5(9)10)1-2-4(7)8/h3H,1-2,6H2,(H,7,8)(H,9,10)/t3-/m0/s1
InChIKeyWHUUTDBJXJRKMK-VKHMYHEASA-N
SMILES
SoftwareSMILES
ACDLabs 12.01O=C(O)C(N)CCC(=O)O
OpenEye OEToolkits 1.7.0C(CC(=O)O)C(C(=O)O)N
OpenEye OEToolkits 1.7.0C(CC(=O)O)[C@@H](C(=O)O)N
CACTVS 3.370N[C@@H](CCC(O)=O)C(O)=O
CACTVS 3.370N[CH](CCC(O)=O)C(O)=O
FormulaC5 H9 N O4
NameGLUTAMIC ACID
ChEMBLCHEMBL575060
DrugBankDB00142
ZINCZINC000001482113
PDB chain6dhd Chain B Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB6dhd Structures of bovine glutamate dehydrogenase complexes elucidate the mechanism of purine regulation.
Resolution2.5 Å
Binding residue
(original residue number in PDB)		K90 M111 K114 K126 A166 G377 V378 S381
Binding residue
(residue number reindexed from 1)		K90 M111 K114 K126 A166 G377 V378 S381
Annotation score5
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)(+)].
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6dhd, PDBe:6dhd, PDBj:6dhd
PDBsum6dhd
PubMed11254391
UniProtP00366|DHE3_BOVIN Glutamate dehydrogenase 1, mitochondrial (Gene Name=GLUD1)

[Back to BioLiP]