Structure of PDB 2jjh Chain A Binding Site BS02

Receptor Information
>2jjh Chain A (length=435) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TTPDRVHEVLGRSMLVDGLDIVLDLTRSGGSYLVDAITGRRYLDMFTFVA
SSALGMNPPALVDDREFHAELMQAALNKPSNSDVYSVAMARFVETFARVL
GDPALPHLFFVEGGALAVENALKAAFDWKSRHNQAHGIDPALGTQVLHLR
GAFHGRSGYTLSLTNTKPTITARFPKFDWPRIDAPYMRPGLDEPAMAALE
AEALRQARAAFETRPHDIACFVAEPIQGAGGDRHFRPEFFAAMRELCDEF
DALLIFDEVQTGCGLTGTAWAYQQLDVAPDIVAFGKKTQVCGVMAGRRVD
EVADNVFAVPSRLNSTWGGNLTDMVRARRILEVIEAEGLFERAVQHGKYL
RARLDELAADFPAVVLDPRGRGLMCAFSLPTTADRDELIRQLWQRAVIVL
PAGADTVRFRPPLTVSTAEIDAAIAAVRSALPVVT
Ligand information
Ligand IDAKG
InChIInChI=1S/C5H6O5/c6-3(5(9)10)1-2-4(7)8/h1-2H2,(H,7,8)(H,9,10)
InChIKeyKPGXRSRHYNQIFN-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=C(O)C(=O)CCC(=O)O
OpenEye OEToolkits 1.7.6C(CC(=O)O)C(=O)C(=O)O
CACTVS 3.385OC(=O)CCC(=O)C(O)=O
FormulaC5 H6 O5
Name2-OXOGLUTARIC ACID
ChEMBLCHEMBL1686
DrugBankDB08845
ZINCZINC000001532519
PDB chain2jjh Chain A Residue 1451 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2jjh Mutational Analysis of Mycobacterium Tuberculosis Lysine Epsilon-Aminotransferase and Inhibitor Co-Crystal Structures, Reveals Distinct Binding Modes.
Resolution2.7 Å
Binding residue
(original residue number in PDB)		F167 R170 A243 R422
Binding residue
(residue number reindexed from 1)		F153 R156 A229 R408
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) V20 F167 E238 D271 Q274 K300 T330 R422
Catalytic site (residue number reindexed from 1) V6 F153 E224 D257 Q260 K286 T316 R408
Enzyme Commision number 2.6.1.36: L-lysine 6-transaminase.
Gene Ontology
Molecular Function
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0045484 L-lysine 6-transaminase activity
Biological Process
GO:0009450 gamma-aminobutyric acid catabolic process
GO:0017000 antibiotic biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2jjh, PDBe:2jjh, PDBj:2jjh
PDBsum2jjh
PubMed26003725
UniProtP9WQ77|LAT_MYCTU Probable L-lysine-epsilon aminotransferase (Gene Name=lat)

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