Structure of PDB 3anu Chain A Binding Site BS02
Receptor Information
>3anu Chain A (length=367) Species:
9031
(Gallus gallus) [
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MWLGALLDTLPTPALTIDRTTARRNAERMRERCRALGVRLRPHVKTHKTL
EGGLLATGGTRRGIAVSTLAEARFFADGGFDDILLAYPVPTARLEECAGL
ARRLDAFHVLLDRPEALASLRQRPLGHGKRWLVWLKLDCGRAGVRPTDPA
ALELAQAIANDAPEEVTLVGVYAHCGNTYCSGADTIQAIARTTTNAVLSF
VAALRQAGVPCPQASIGSTPSCSHPIPEMSQLTELHPGNYIFYDLQQTQL
GSCQPQDVAIRVLTRVIGHYAHRGQLLVDCGWAALSLHGAGGPQGCAAID
GHPELRLVGLTQEHGLLEHQMDFGRFPVGSVLALIPYHACATAAMHPVYY
VHEEGKVVALWHPVRGW
Ligand information
Ligand ID
ZN
InChI
InChI=1S/Zn/q+2
InChIKey
PTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
Formula
Zn
Name
ZINC ION
ChEMBL
CHEMBL1236970
DrugBank
DB14532
ZINC
PDB chain
3anu Chain A Residue 451 [
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Receptor-Ligand Complex Structure
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PDB
3anu
Crystal structure of a zinc-dependent D-serine dehydratase from chicken kidney
Resolution
1.9 Å
Binding residue
(original residue number in PDB)
H347 C349
Binding residue
(residue number reindexed from 1)
H338 C340
Annotation score
1
Enzymatic activity
Enzyme Commision number
4.3.1.18
: D-serine ammonia-lyase.
Gene Ontology
Molecular Function
GO:0008270
zinc ion binding
GO:0008721
D-serine ammonia-lyase activity
GO:0016829
lyase activity
GO:0030170
pyridoxal phosphate binding
GO:0046872
metal ion binding
Biological Process
GO:0036088
D-serine catabolic process
Cellular Component
GO:0005737
cytoplasm
GO:0030425
dendrite
GO:0042995
cell projection
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Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:3anu
,
PDBe:3anu
,
PDBj:3anu
PDBsum
3anu
PubMed
21676877
UniProt
A0A8V1ABE9
|DSD1_CHICK D-serine dehydratase (Gene Name=DSD)
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