Structure of PDB 1m32 Chain E

Receptor sequence
>1m32E (length=361) [Search protein sequence]
YLLLTPGPLTTSRTVKEAMLFDSCTWDDDYNIGVVEQIRQQLTALATASE
GYTSVLLQGSGSYAVEAVLGSALGPQDKVLIVSNGAYGARMVEMAGLMGI
AHHAYDCGEVARPDVQAIDAILNADPTISHIAMVHSETTTGMLNPIDEVG
ALAHRYGKTYIVDAMSSFGGIPMDIAALHIDYLISSANKCIQGVPGFAFV
IAREQKLAACKGHSRSLSLDLYAQWRCMEDNHGKWRFTSPTHTVLAFAQA
LKELAKEGGVAARHQRYQQNQRSLVAGMRALGFNTLLDDELHSPIITAFY
SPEDPQYRFSEFYRRLKEQGFVIYPGKVSQSDCFRIGNIGEVYAADITAL
LTAIRTAMYWT
3D structure
PDB1m32 Degradation Pathway of the Phosphonate Ciliatine: Crystal Structure of 2-Aminoethylphosphonate Transaminase
ChainE
Resolution2.2 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.6.1.37: 2-aminoethylphosphonate--pyruvate transaminase.
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 PO4 E Y91 Y328 Y87 Y324
BS02 PLP E S64 G65 S66 Y91 T142 D167 M169 S60 G61 S62 Y87 T138 D163 M165
BS03 PLP E F241 T242 F237 T238
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
View graph for
Biological Process
External links
PDB RCSB:1m32, PDBe:1m32, PDBj:1m32
PDBsum1m32
PubMed12403617
UniProtP96060|PHNW_SALTY 2-aminoethylphosphonate--pyruvate transaminase (Gene Name=phnW)

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