Structure of PDB 3wqe Chain A

Receptor sequence
>3wqeA (length=379) Species: 518882 (Delftia sp. HT23) [Search protein sequence]
QDTLLTLDTPAAVIDLDRMQRNIARMQQRMDAQGVRLRPHVKTSKSVPVA
AAQRAAGASGITVSTLKEAEQFFAAGTTDILYAVSMAPHRLPQALQLRRR
GCDLKLIVDSVAAAQAIAAFGREQGEAFEVWIEIDTDGHRSGVGADDTPL
LLAIGRTLHDGGMRLGGVLTHAGSSYELDTPEALQALAERERAGCVQAAE
ALRAAGLPCPVVSVGSTPTALAASRLDGVTEVRAGVYVFFDLVMRNIGVC
AAEDVALSVLATVIGHQADKGWAIVDAGWMAMSRDRGTARQKQDFGYGQV
CDLQGRVMPGFVLTGANQEHGILARADGAAEADIATRFPLGTRLRILPNH
ACATGAQFPAYQALAADGSVQTWERLHGW
3D structure
PDB3wqe 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
Resolution1.6 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 T218 R234 A235 G236 V237 H40 K42 R140 H171 Y176 T217 R233 A234 G235 V236
BS02 MG A H351 C353 H350 C352
BS03 2TL A H140 R141 H172 H139 R140 H171
BS04 2TL A N318 Q319 N317 Q318
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
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Biological Process
External links
PDB RCSB:3wqe, PDBe:3wqe, PDBj:3wqe
PDBsum3wqe
PubMed25715785
UniProtB2DFG5|DTHAD_DELSH D-threo-3-hydroxyaspartate dehydratase (Gene Name=dthadh)

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