Structure of PDB 1pym Chain A

Receptor sequence
>1pymA (length=291) Species: 6550 (Mytilus edulis) [Search protein sequence]
VKKTTQLKQMLNSKDLEFIMEAHNGLSARIVQEAGFKGIWGSGLSVSAQL
GVRDSNEASWTQVVEVLEFMSDASDVPILLDADTGYGNFNNARRLVRKLE
DRGVAGACLEDKLFPKTNSLHDGRAQPLADIEEFALKIKACKDSQTDPDF
CIVARVEAFIAGWGLDEALKRAEAYRNAGADAILMHSKKADPSDIEAFMK
AWNNQGPVVIVPTKYYKTPTDHFRDMGVSMVIWANHNLRASVSAIQQTTK
QIYDDQSLVNVEDKIVSVKEIFRLQRDDELVQAEDKYLPKN
3D structure
PDB1pym Helix swapping between two alpha/beta barrels: crystal structure of phosphoenolpyruvate mutase with bound Mg(2+)-oxalate.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) W44 S46 G47 L48 D58 D85 D87 C112 E114 K120 N122 S123 R159 H190 V215
Catalytic site (residue number reindexed from 1) W40 S42 G43 L44 D54 D81 D83 C108 E110 K116 N118 S119 R155 H186 V211
Enzyme Commision number 5.4.2.9: phosphoenolpyruvate mutase.
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 OXL A W44 S46 G47 L48 D85 R159 W40 S42 G43 L44 D81 R155
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016853 isomerase activity
GO:0046872 metal ion binding
GO:0050188 phosphoenolpyruvate mutase activity
Biological Process
GO:0032923 organic phosphonate biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1pym, PDBe:1pym, PDBj:1pym
PDBsum1pym
PubMed10378273
UniProtP56839|PEPM_MYTED Phosphoenolpyruvate phosphomutase

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