Structure of PDB 3lqs Chain A

Receptor sequence
>3lqsA (length=280) Species: 72579 (Bacillus sp. YM-1) [Search protein sequence]
GYTLWNDQIVKDEEVKIDKEDRGYQFGDGVYEVVKVYNGEMFTVNEHIDR
LYASAEKIRITIPYTKDKFHQLLHELVEKNELNTGHIYFQVTRGTSPRAH
QFPENTVKPVIIGYTKENPRPLENLEKGVKATFVEDIRWLRCDIKSLNLL
GAVLAKQEAHEKGCYEAILHRNNTVTEGSSSNVFGIKDGILYTHPANNMI
LKGITRDVVIACANEINMPVKEIPFTTHEALKMDELFVTSTTSEITPVIE
IDGKLIRDGKVGEWTRKLQKQFETKIPKPL
3D structure
PDB3lqs Chiral discrimination among aminotransferases: inactivation by 4-amino-4,5-dihydrothiophenecarboxylic acid.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y31 V33 K145 E177 L201
Catalytic site (residue number reindexed from 1) Y31 V33 K145 E177 L201
Enzyme Commision number 2.6.1.21: D-amino-acid 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 PSZ A V33 R50 E177 S180 S181 N182 L201 G203 I204 T205 S240 T241 T242 V33 R50 E177 S180 S181 N182 L201 G203 I204 T205 S240 T241 T242
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0047810 D-alanine-2-oxoglutarate aminotransferase activity
Biological Process
GO:0019478 D-amino acid catabolic process
GO:0019752 carboxylic acid metabolic process
GO:0046394 carboxylic acid biosynthetic process
GO:0046416 D-amino acid metabolic process
GO:0046437 D-amino acid biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3lqs, PDBe:3lqs, PDBj:3lqs
PDBsum3lqs
PubMed20192272
UniProtP19938|DAAA_BACYM D-alanine aminotransferase (Gene Name=dat)

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