Structure of PDB 4v15 Chain A Binding Site BS03
Receptor Information
>4v15 Chain A (length=373) Species:
85698
(Achromobacter xylosoxidans) [
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RGIALPPAAQPGDPLARVDTPSLVLDLPAFEANLRAMQAWADRHEVALRP
HAKAHKCPEIALRQLALGARGICCQKVSEALPFVAAGIRDIHISNEVVGP
AKLALLGQLARAAKISVCVDNAENLAQLSAAMTRAGAEIDVLVEVDVGQG
RCGVSDDATVLALAQQARALPGLNFAGLQAYHGSVQHYRTREERAAVCRQ
AARIAASYAQLLRESGIACDTITGGGTGSVEFDAASGVYTELQAGSYAFM
DSDYGANEWNGPLKFQNSLFVLSTVMSTPAPGRVILDAGLKSTTAECGPP
AVYGEPGLTYAAINDEHGVVRVEPGAQAPALGAVLRLVPSHVDPTFNLHD
GLVVVKDGVVQDVWEIAARGFSR
Ligand information
Ligand ID
MN
InChI
InChI=1S/Mn/q+2
InChIKey
WAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341
[Mn++]
Formula
Mn
Name
MANGANESE (II) ION
ChEMBL
DrugBank
DB06757
ZINC
PDB chain
4v15 Chain A Residue 1382 [
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Receptor-Ligand Complex Structure
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PDB
4v15
The Crystal Structure of D-Threonine Aldolase from Alcaligenes Xylosoxidans Provides Insight Into a Metal Ion Assisted Plp-Dependent Mechanism.
Resolution
1.5 Å
Binding residue
(original residue number in PDB)
H347 D349
Binding residue
(residue number reindexed from 1)
H341 D343
Annotation score
1
Enzymatic activity
Enzyme Commision number
4.1.2.42
: D-threonine aldolase.
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
PDBsum
4v15
PubMed
25884707
UniProt
A0A0J9X243
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