Structure of PDB 4pb5 Chain B

Receptor sequence
>4pb5B (length=388) Species: 518882 (Delftia sp. HT23) [Search protein sequence]
HHHHHAMSMQDTLLTLDTPAAVIDLDRMQRNIARMQQRMDAQGVRLRPHV
KTSKSVPVAAAQRAAGASGITVSTLKEAEQFFAAGTTDILYAVSMAPHRL
PQALQLRRRGCDLKLIVDSVAAAQAIAAFGREQGEAFEVWIEIDTDGHRS
GVGADDTPLLLAIGRTLHDGGMRLGGVLTHAGSSYELDTPEALQALAERE
RAGCVQAAEALRAAGLPCPVVSVGSTPTALAASRLDGVTEVRAGVYVFFD
LVMRNIGVCAAEDVALSVLATVIGHQADKGWAIVDAGWMAMSRDRGTARQ
KQDFGYGQVCDLQGRVMPGFVLTGANQEHGILARADGAAEADIATRFPLG
TRLRILPNAACATGAQFPAYQALAADGSVQTWERLHGW
3D structure
PDB4pb5 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.
ChainB
Resolution1.9 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 BH2 B N318 Q319 N326 Q327
BS02 PLP B H41 K43 R141 H172 Y177 S217 T218 R234 A235 G236 H49 K51 R149 H180 Y185 S225 T226 R242 A243 G244
BS03 BH2 B K43 R141 H172 Y177 K51 R149 H180 Y185
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:4pb5, PDBe:4pb5, PDBj:4pb5
PDBsum4pb5
PubMed25715785
UniProtB2DFG5|DTHAD_DELSH D-threo-3-hydroxyaspartate dehydratase (Gene Name=dthadh)

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