Structure of PDB 2cjg Chain A

Receptor sequence
>2cjgA (length=435) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
TTPDRVHEVLGRSMLVDGLDIVLDLTRSGGSYLVDAITGRRYLDMFTFVA
SSALGMNPPALVDDREFHAELMQAALNKPSNSDVYSVAMARFVETFARVL
GDPALPHLFFVEGGALAVENALKAAFDWKSRHNQAHGIDPALGTQVLHLR
GAFHGRSGYTLSLTNTKPTITARFPKFDWPRIDAPYMRPGLDEPAMAALE
AEALRQARAAFETRPHDIACFVAEPIQGEGGDRHFRPEFFAAMRELCDEF
DALLIFDEVQTGCGLTGTAWAYQQLDVAPDIVAFGKKTQVCGVMAGRRVD
EVADNVFAVPSRLNSTWGGNLTDMVRARRILEVIEAEGLFERAVQHGKYL
RARLDELAADFPAVVLDPRGRGLMCAFSLPTTADRDELIRQLWQRAVIVL
PAGADTVRFRPPLTVSTAEIDAAIAAVRSALPVVT
3D structure
PDB2cjg Direct Evidence for a Glutamate Switch Necessary for Substrate Recognition: Crystal Structures of Lysine Epsilon-Aminotransferase (Rv3290C) from Mycobacterium Tuberculosis H37Rv.
ChainA
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 PMP A G128 A129 F167 H168 E238 D271 V273 K300 G114 A115 F153 H154 E224 D257 V259 K286
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:2cjg, PDBe:2cjg, PDBj:2cjg
PDBsum2cjg
PubMed16950391
UniProtP9WQ77|LAT_MYCTU Probable L-lysine-epsilon aminotransferase (Gene Name=lat)

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