Structure of PDB 1a0g Chain A

Receptor sequence

>1a0gA (length=280) Species: 72579 (Bacillus sp. YM-1)

GYTLWNDQIVKDEEVKIDKEDRGYQFGDGVYEVVKVYNGEMFTVNEHIDR
LYASAEKIRITIPYTKDKFHQLLHELVEKNELNTGHIYFQVTRGTSPRAH
QFPENTVKPVIIGYTKENPRPLENLEKGVKATFVEDIRWLRCDIKSLNLL
GAVLAKQEAHEKGCYEAILHRNNTVTEGSSSNVFGIKDGILYTHPANNMI
AKGITRDVVIACANEINMPVKEIPFTTHEALKMDELFVTSTTSEITPVIE
IDGKLIRDGKVGEWTRKLQKQFETKIPKPL

3D structure

• PDB: 1a0g Crystal structures of L201A mutant of D-amino acid aminotransferase at 2.0 A resolution: implication of the structural role of Leu201 in transamination.
• Chain: A
• Resolution: 2.0 Å

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	A	Y31 R50 K145 E177 S180 S181 A201 G203 T205 S240 T241	Y31 R50 K145 E177 S180 S181 A201 G203 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

External links

• PDB: RCSB:1a0g, PDBe:1a0g, PDBj:1a0g
• PDBsum: 1a0g
• PubMed: 9749913
• UniProt: P19938|DAAA_BACYM D-alanine aminotransferase (Gene Name=dat)