Structure of PDB 3aog Chain I Binding Site BS03

Receptor Information
>3aog Chain I (length=421) Species: 262724 (Thermus thermophilus HB27) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EPLSYLGKDGGPWEIFTEQVDRVVPYLGRLAPLAESLKRPKRVLIVDVPV
RLDDGSVAYFEGYRVHHNTARGPAKGGVRYHPEVTLSEVMALAGWMTIKN
AAVGLPYGGGKGGIRVDPRKLSPGELERLTRRYTSEIGILLGPDRDIPAP
DVNTGEREMAWMMDTYSMNVGRTVPGVVTGKPIALGGSLGRRDATGRGVF
ITAAAAAEKIGLQVEGARVAIQGFGNVGNAAARAFHDHGARVVAVQDHTG
TVYNEAGIDPYDLLRHVQEFGGVRGYPKAEPLPAADFWGLPVEFLVPAAL
EKQITEQNAWRIRARIVAEGANGPTTPAADDILLEKGVLVVPDVIANAGG
VTVSYFEWVQDFNSYFWTEEEINARLERVLRNAFEAVWQVAQEKKIPLRT
AAYVVAATRVLEARALRGLYP
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 chain3aog Chain I Residue 425 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3aog An unique allosteric regulation revealed by crystal structure of hetero-hexameric glutamate dehydrogenase from Thermus thermophilus
Resolution2.1 Å
Binding residue
(original residue number in PDB)		A73 R420 G421 L422 Y423
Binding residue
(residue number reindexed from 1)		A70 R417 G418 L419 Y420
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) K114 D154
Catalytic site (residue number reindexed from 1) K111 D151
Enzyme Commision number 1.4.1.3: glutamate dehydrogenase [NAD(P)(+)].
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004352 glutamate dehydrogenase (NAD+) activity
GO:0004353 glutamate dehydrogenase [NAD(P)+] 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:0006538 glutamate catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3aog, PDBe:3aog, PDBj:3aog
PDBsum3aog
PubMed
UniProtQ72IC1

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