Structure of PDB 3wqf Chain A

Receptor sequence
>3wqfA (length=378) Species: 518882 (Delftia sp. HT23) [Search protein sequence]
DTLLTLDTPAAVIDLDRMQRNIARMQQRMDAQGVRLRPHVKTSKSVPVAA
AQRAAGASGITVSTLKEAEQFFAAGTTDILYAVSMAPHRLPQALQLRRRG
CDLKLIVDSVAAAQAIAAFGREQGEAFEVWIEIDTDGHRSGVGADDTPLL
LAIGRTLHDGGMRLGGVLTHAGSSYELDTPEALQALAERERAGCVQAAEA
LRAAGLPCPVVSVGSTPTALAASRLDGVTEVRAGVYVFFDLVMRNIGVCA
AEDVALSVLATVIGHQADKGWAIVDAGWMAMSRDRGTARQKQDFGYGQVC
DLQGRVMPGFVLTGANQEHGILARADGAAEADIATRFPLGTRLRILPNHA
CATGAQFPAYQALAADGSVQTWERLHGW
3D structure
PDB3wqf Structural insights into the substrate stereospecificity of D-threo-3-hydroxyaspartate dehydratase from Delftia sp. HT23: a useful enzyme for the synthesis of optically pure L-threo- and D-erythro-3-hydroxyaspartate
ChainA
Resolution2.3 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.3.1.27: threo-3-hydroxy-D-aspartate ammonia-lyase.
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 H41 K43 R141 H172 Y177 S217 T218 R234 A235 G236 H39 K41 R139 H170 Y175 S215 T216 R232 A233 G234
Gene Ontology
Molecular Function
GO:0008721 D-serine ammonia-lyase activity
GO:0016829 lyase activity
GO:0016841 ammonia-lyase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0036088 D-serine catabolic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3wqf, PDBe:3wqf, PDBj:3wqf
PDBsum3wqf
PubMed25715785
UniProtB2DFG5|DTHAD_DELSH D-threo-3-hydroxyaspartate dehydratase (Gene Name=dthadh)

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