Structure of PDB 4v15 Chain A

Receptor sequence
>4v15A (length=373) Species: 85698 (Achromobacter xylosoxidans) [Search protein sequence]
RGIALPPAAQPGDPLARVDTPSLVLDLPAFEANLRAMQAWADRHEVALRP
HAKAHKCPEIALRQLALGARGICCQKVSEALPFVAAGIRDIHISNEVVGP
AKLALLGQLARAAKISVCVDNAENLAQLSAAMTRAGAEIDVLVEVDVGQG
RCGVSDDATVLALAQQARALPGLNFAGLQAYHGSVQHYRTREERAAVCRQ
AARIAASYAQLLRESGIACDTITGGGTGSVEFDAASGVYTELQAGSYAFM
DSDYGANEWNGPLKFQNSLFVLSTVMSTPAPGRVILDAGLKSTTAECGPP
AVYGEPGLTYAAINDEHGVVRVEPGAQAPALGAVLRLVPSHVDPTFNLHD
GLVVVKDGVVQDVWEIAARGFSR
3D structure
PDB4v15 The Crystal Structure of D-Threonine Aldolase from Alcaligenes Xylosoxidans Provides Insight Into a Metal Ion Assisted Plp-Dependent Mechanism.
ChainA
Resolution1.5 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.1.2.42: D-threonine aldolase.
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 H57 K59 Y187 T233 Q249 A250 S252 Y260 H51 K53 Y181 T227 Q243 A244 S246 Y254
BS02 PLP A H57 K59 Q81 S100 Y187 G232 T233 Q249 G251 S252 Y260 H51 K53 Q75 S94 Y181 G226 T227 Q243 G245 S246 Y254
BS03 MN A H347 D349 H341 D343
Gene Ontology
Molecular Function
GO:0008721 D-serine ammonia-lyase activity
GO:0016829 lyase activity
GO:0043876 D-threonine aldolase activity
GO:0046872 metal ion 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:4v15, PDBe:4v15, PDBj:4v15
PDBsum4v15
PubMed25884707
UniProtA0A0J9X243

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