Structure of PDB 5daa Chain A

Receptor sequence
>5daaA (length=277) Species: 72579 (Bacillus sp. YM-1) [Search protein sequence]
GYTLWNDQIVKDEEVKIDKEDRGYQFGDGVYEVVKVYNGEMFTVNEHIDR
LYASAEKIRITIPYTKDKFHQLLHELVEKNELNTGHIYFQVTRGTSPRAH
QFPENTVKPVIIGYTKENPRPLENLEKGVKATFVEDIRWLRCDIKSLNLL
GAVLAKQEAHEKGCYEAILHRNNTVTKGSSSNVFGIKDGILYTHPANNMI
LKGITRDVVIACANEINMPVKEIPFTTHEALKMDELFVTSTTSEITPVIE
IDGKLIRDGKVGEWTRKLQKQFETKIP
3D structure
PDB5daa Effects of the E177K mutation in D-amino acid transaminase. Studies on an essential coenzyme anchoring group that contributes to stereochemical fidelity.
ChainA
Resolution2.9 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 K177 L201
Catalytic site (residue number reindexed from 1) Y31 V33 K145 K177 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 S181 L201 G203 I204 T205 T241 R50 K145 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

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Molecular Function
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Biological Process
External links
PDB RCSB:5daa, PDBe:5daa, PDBj:5daa
PDBsum5daa
PubMed9930994
UniProtP19938|DAAA_BACYM D-alanine aminotransferase (Gene Name=dat)

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