Structure of PDB 1g2w Chain A

Receptor sequence

>1g2wA (length=277) Species: 1422 (Geobacillus stearothermophilus)

GYTLWNDQIVKDEEVKIDKEDRGYQFGDGVYEVVKVYNGEMFTVNEHIDR
LYASAEKIRITIPYTKDKFHQLLHELVEKNELNTGHIYFQVTRGTSPRAH
QFPENTVKPVIIGYTKENPRPLENLEKGVKATFVEDIRWLRCDIKSLNLL
GAVLAKQEAHEKGCYEAILHRNNTVTSGSSSNVFGIKDGILYTHPANNMI
LKGITRDVVIACANEINMPVKEIPFTTHEALKMDELFVTSTTSEITPVIE
IDGKLIRDGKVGEWTRKLQKQFETKIP

3D structure

• PDB: 1g2w Effects of the E177K mutation in D-amino acid aminotransaminase. Studies on an essential coenzyme anchoring group that contributes to stereochemical fidelity
• Chain: A
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y31 V33 K145 S177 L201
• Catalytic site (residue number reindexed from 1): Y31 V33 K145 S177 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	PLP	A	R50 K145 S180 S181 L201 G203 I204 T205 T241	R50 K145 S180 S181 L201 G203 I204 T205 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:1g2w, PDBe:1g2w, PDBj:1g2w
• PDBsum: 1g2w
• UniProt: P19938|DAAA_BACYM D-alanine aminotransferase (Gene Name=dat)