Structure of PDB 2jjh Chain A

Receptor sequence
>2jjhA (length=435) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence]
TTPDRVHEVLGRSMLVDGLDIVLDLTRSGGSYLVDAITGRRYLDMFTFVA
SSALGMNPPALVDDREFHAELMQAALNKPSNSDVYSVAMARFVETFARVL
GDPALPHLFFVEGGALAVENALKAAFDWKSRHNQAHGIDPALGTQVLHLR
GAFHGRSGYTLSLTNTKPTITARFPKFDWPRIDAPYMRPGLDEPAMAALE
AEALRQARAAFETRPHDIACFVAEPIQGAGGDRHFRPEFFAAMRELCDEF
DALLIFDEVQTGCGLTGTAWAYQQLDVAPDIVAFGKKTQVCGVMAGRRVD
EVADNVFAVPSRLNSTWGGNLTDMVRARRILEVIEAEGLFERAVQHGKYL
RARLDELAADFPAVVLDPRGRGLMCAFSLPTTADRDELIRQLWQRAVIVL
PAGADTVRFRPPLTVSTAEIDAAIAAVRSALPVVT
3D structure
PDB2jjh Mutational Analysis of Mycobacterium Tuberculosis Lysine Epsilon-Aminotransferase and Inhibitor Co-Crystal Structures, Reveals Distinct Binding Modes.
ChainA
Resolution2.7 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 PLP A G128 A129 F167 H168 E238 D271 V273 Q274 K300 G114 A115 F153 H154 E224 D257 V259 Q260 K286
BS02 AKG A F167 R170 A243 R422 F153 R156 A229 R408
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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