Structure of PDB 1m1b Chain A

Receptor sequence
>1m1bA (length=291) Species: 6550 (Mytilus edulis) [Search protein sequence]
VKKTTQLKQMLNSKDLEFIMEAHNGLSARIVQEAGFKGIWGSGLSVSAQL
GVRDSNEASWTQVVEVLEFMSDASDVPILLDADTGYGNFNNARRLVRKLE
DRGVAGACLEDKLFPKTNSLHDGRAQPLADIEEFALKIKACKDSQTDPDF
CIVARVEAFIAGWGLDEALKRAEAYRNAGADAILMHSKKADPSDIEAFMK
AWNNQGPVVIVPTKYYKTPTDHFRDMGVSMVIWANHNLRASVSAIQQTTK
QIYDDQSLVNVEDKIVSVKEIFRLQRDDELVQAEDKYLPKN
3D structure
PDB1m1b Dissociative phosphoryl transfer in PEP mutase catalysis: structure of the enzyme/sulfopyruvate complex and kinetic properties of mutants.
ChainA
Resolution2.25 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 MG A D85 R159 D81 R155
BS02 SPV A S46 G47 L48 D85 N122 S123 L124 R159 S42 G43 L44 D81 N118 S119 L120 R155 MOAD: Ki=22uM
PDBbind-CN: -logKd/Ki=4.66,Ki=22uM
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]