Structure of PDB 1m1b Chain A Binding Site BS02

Receptor Information
>1m1b Chain A (length=291) 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
QIYDDQSLVNVEDKIVSVKEIFRLQRDDELVQAEDKYLPKN
Ligand information
Ligand IDSPV
InChIInChI=1S/C3H4O6S/c4-2(3(5)6)1-10(7,8)9/h1H2,(H,5,6)(H,7,8,9)
InChIKeyBUTHMSUEBYPMKJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341OC(=O)C(=O)C[S](O)(=O)=O
ACDLabs 10.04O=C(O)C(=O)CS(=O)(=O)O
OpenEye OEToolkits 1.5.0C(C(=O)C(=O)O)S(=O)(=O)O
FormulaC3 H4 O6 S
NameSULFOPYRUVATE
ChEMBL
DrugBankDB02156
ZINCZINC000004096823
PDB chain1m1b Chain A Residue 996 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1m1b Dissociative phosphoryl transfer in PEP mutase catalysis: structure of the enzyme/sulfopyruvate complex and kinetic properties of mutants.
Resolution2.25 Å
Binding residue
(original residue number in PDB)		S46 G47 L48 D85 N122 S123 L124 R159
Binding residue
(residue number reindexed from 1)		S42 G43 L44 D81 N118 S119 L120 R155
Annotation score1
Binding affinityMOAD: Ki=22uM
PDBbind-CN: -logKd/Ki=4.66,Ki=22uM
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
View graph for
Biological Process
External links
PDB RCSB:1m1b, PDBe:1m1b, PDBj:1m1b
PDBsum1m1b
PubMed12162742
UniProtP56839|PEPM_MYTED Phosphoenolpyruvate phosphomutase

[Back to BioLiP]