Structure of PDB 1a0g Chain B

Receptor sequence
>1a0gB (length=282) Species: 72579 (Bacillus sp. YM-1) [Search protein sequence]
GYTLWNDQIVKDEEVKIDKEDRGYQFGDGVYEVVKVYNGEMFTVNEHIDR
LYASAEKIRITIPYTKDKFHQLLHELVEKNELNTGHIYFQVTRGTSPRAH
QFPENTVKPVIIGYTKENPRPLENLEKGVKATFVEDIRWLRCDIKSLNLL
GAVLAKQEAHEKGCYEAILHRNNTVTEGSSSNVFGIKDGILYTHPANNMI
AKGITRDVVIACANEINMPVKEIPFTTHEALKMDELFVTSTTSEITPVIE
IDGKLIRDGKVGEWTRKLQKQFETKIPKPLHI
3D structure
PDB1a0g Crystal structures of L201A mutant of D-amino acid aminotransferase at 2.0 A resolution: implication of the structural role of Leu201 in transamination.
ChainB
Resolution2.0 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 A201
Catalytic site (residue number reindexed from 1) Y31 V33 K145 E177 A201
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 PMP B R50 K145 E177 S180 S181 G203 I204 T205 S240 T241 R50 K145 E177 S180 S181 G203 I204 T205 S240 T241
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:1a0g, PDBe:1a0g, PDBj:1a0g
PDBsum1a0g
PubMed9749913
UniProtP19938|DAAA_BACYM D-alanine aminotransferase (Gene Name=dat)

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