Structure of PDB 1m32 Chain E Binding Site BS03
Receptor Information
>1m32 Chain E (length=361) [
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YLLLTPGPLTTSRTVKEAMLFDSCTWDDDYNIGVVEQIRQQLTALATASE
GYTSVLLQGSGSYAVEAVLGSALGPQDKVLIVSNGAYGARMVEMAGLMGI
AHHAYDCGEVARPDVQAIDAILNADPTISHIAMVHSETTTGMLNPIDEVG
ALAHRYGKTYIVDAMSSFGGIPMDIAALHIDYLISSANKCIQGVPGFAFV
IAREQKLAACKGHSRSLSLDLYAQWRCMEDNHGKWRFTSPTHTVLAFAQA
LKELAKEGGVAARHQRYQQNQRSLVAGMRALGFNTLLDDELHSPIITAFY
SPEDPQYRFSEFYRRLKEQGFVIYPGKVSQSDCFRIGNIGEVYAADITAL
LTAIRTAMYWT
Ligand information
Ligand ID
PLP
InChI
InChI=1S/C8H10NO6P/c1-5-8(11)7(3-10)6(2-9-5)4-15-16(12,13)14/h2-3,11H,4H2,1H3,(H2,12,13,14)
InChIKey
NGVDGCNFYWLIFO-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
Cc1ncc(CO[P](O)(O)=O)c(C=O)c1O
OpenEye OEToolkits 1.5.0
Cc1c(c(c(cn1)COP(=O)(O)O)C=O)O
ACDLabs 10.04
O=P(O)(O)OCc1cnc(c(O)c1C=O)C
Formula
C8 H10 N O6 P
Name
PYRIDOXAL-5'-PHOSPHATE;
VITAMIN B6 Phosphate
ChEMBL
CHEMBL82202
DrugBank
DB00114
ZINC
ZINC000001532514
PDB chain
1m32 Chain F Residue 4406 [
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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)
F241 T242
Binding residue
(residue number reindexed from 1)
F237 T238
Annotation score
1
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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