Structure of PDB 3uzo Chain A Binding Site BS02

Receptor Information
>3uzo Chain A (length=335) Species: 1299 (Deinococcus radiodurans) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
IDWSTLGFSYIRTDLRYLAHWKDGEWDAGTLTEDNQIHLAEGSTALHYGQ
QCFEGLKAYRCADGSINLFRPDQNAARMRMSCRRLLMPELSDEQFIDACL
QVVRANEHFLPPYGTGGSLYLRPFVIGVGDNIGVRTAPEFIFSVFCVPVG
PYFKGGLTPTNFITSDYDRAAPHGTGAAKVGGNYAASLLPGYEAKKRDFA
DVIYLDPATHTTIEEAGAANFFAITQDGQKFVTPQSPSILPSITKYSLLW
LAEHRLGLEVEEGDIRIDELGKFSEAGACGTAAVITPIGGIQHGDDFHVF
YSESEPGPVTRRLYDELVGIQYGDKEAPEGWIVKV
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 chain3uzo Chain A Residue 600 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3uzo Crystal Structures of Complexes of the Branched-Chain Aminotransferase from Deinococcus radiodurans with alpha-Ketoisocaproate and L-Glutamate Suggest the Radiation Resistance of This Enzyme for Catalysis
Resolution2.0 Å
Binding residue
(original residue number in PDB)
F76 R145 Y175 T304 A305
Binding residue
(residue number reindexed from 1)
F53 R122 Y152 T281 A282
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) K202
Catalytic site (residue number reindexed from 1) K179
Enzyme Commision number 2.6.1.42: branched-chain-amino-acid transaminase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004084 branched-chain-amino-acid transaminase activity
GO:0008483 transaminase activity
GO:0052654 L-leucine-2-oxoglutarate transaminase activity
GO:0052655 L-valine-2-oxoglutarate transaminase activity
GO:0052656 L-isoleucine-2-oxoglutarate transaminase activity
Biological Process
GO:0008652 amino acid biosynthetic process
GO:0009081 branched-chain amino acid metabolic process
GO:0009082 branched-chain amino acid biosynthetic process
GO:0009097 isoleucine biosynthetic process
GO:0009098 L-leucine biosynthetic process
GO:0009099 L-valine biosynthetic process

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Molecular Function

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Biological Process
External links
PDB RCSB:3uzo, PDBe:3uzo, PDBj:3uzo
PDBsum3uzo
PubMed22984263
UniProtQ9RTX5

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