Structure of PDB 1m32 Chain A Binding Site BS02
Receptor Information
>1m32 Chain A (length=361) [
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YLLLTPGPLTTSRTVKEAMLFDSCTWDDDYNIGVVEQIRQQLTALATASE
GYTSVLLQGSGSYAVEAVLGSALGPQDKVLIVSNGAYGARMVEMAGLMGI
AHHAYDCGEVARPDVQAIDAILNADPTISHIAMVHSETTTGMLNPIDEVG
ALAHRYGKTYIVDAMSSFGGIPMDIAALHIDYLISSANKCIQGVPGFAFV
IAREQKLAACKGHSRSLSLDLYAQWRCMEDNHGKWRFTSPTHTVLAFAQA
LKELAKEGGVAARHQRYQQNQRSLVAGMRALGFNTLLDDELHSPIITAFY
SPEDPQYRFSEFYRRLKEQGFVIYPGKVSQSDCFRIGNIGEVYAADITAL
LTAIRTAMYWT
Ligand information
Ligand ID
POA
InChI
InChI=1S/C2H5O4P/c3-1-2-7(4,5)6/h1H,2H2,(H2,4,5,6)
InChIKey
YEMKIGUKNDOZEG-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
O[P](O)(=O)CC=O
OpenEye OEToolkits 1.5.0
C(C=O)P(=O)(O)O
ACDLabs 10.04
O=CCP(=O)(O)O
Formula
C2 H5 O4 P
Name
PHOSPHONOACETALDEHYDE
ChEMBL
DrugBank
DB03174
ZINC
PDB chain
1m32 Chain A Residue 4601 [
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Receptor-Ligand Complex Structure
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PDB
1m32
Degradation Pathway of the Phosphonate Ciliatine: Crystal Structure of 2-Aminoethylphosphonate Transaminase
Resolution
2.2 Å
Binding residue
(original residue number in PDB)
Y91 Y328 R339
Binding residue
(residue number reindexed from 1)
Y87 Y324 R335
Annotation score
5
Enzymatic activity
Enzyme Commision number
2.6.1.37
: 2-aminoethylphosphonate--pyruvate transaminase.
Gene Ontology
Molecular Function
GO:0008483
transaminase activity
GO:0047304
2-aminoethylphosphonate-pyruvate transaminase activity
Biological Process
GO:0019700
organic phosphonate catabolic process
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Molecular Function
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Biological Process
External links
PDB
RCSB:1m32
,
PDBe:1m32
,
PDBj:1m32
PDBsum
1m32
PubMed
12403617
UniProt
P96060
|PHNW_SALTY 2-aminoethylphosphonate--pyruvate transaminase (Gene Name=phnW)
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