Structure of PDB 1pym Chain B Binding Site BS01

Receptor Information
>1pym Chain B (length=289) Species: 6550 (Mytilus edulis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VKKTTQLKQMLNSKDLEFIMEAHNGLSARIVQEAGFKGIWGSGLSVSAQL
GVRDSNEASWTQVVEVLEFMSDASDVPILLDADTGYGNFNNARRLVRKLE
DRGVAGACLEDKLFPKTNSLHDGRAQPLADIEEFALKIKACKDSQTDPDF
CIVARVEAFIAGWGLDEALKRAEAYRNAGADAILMHSKKADPSDIEAFMK
AWNNQGPVVIVPTKYYKTPTDHFRDMGVSMVIWANHNLRASVSAIQQTTK
QIYDDQSLVNVEDKIVSVKEIFRLQRDDELVQAEDKYLP
Ligand information
Ligand IDOXL
InChIInChI=1S/C2H2O4/c3-1(4)2(5)6/h(H,3,4)(H,5,6)/p-2
InChIKeyMUBZPKHOEPUJKR-UHFFFAOYSA-L
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341		[O-]C(=O)C([O-])=O
OpenEye OEToolkits 1.5.0C(=O)(C(=O)[O-])[O-]
FormulaC2 O4
NameOXALATE ION
ChEMBL
DrugBank
ZINC
PDB chain1pym Chain B Residue 1002 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1pym Helix swapping between two alpha/beta barrels: crystal structure of phosphoenolpyruvate mutase with bound Mg(2+)-oxalate.
Resolution1.8 Å
Binding residue
(original residue number in PDB)		W44 S46 G47 L48 D85 R159
Binding residue
(residue number reindexed from 1)		W40 S42 G43 L44 D81 R155
Annotation score1
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.
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

View graph for
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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