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1S2W

Crystal structure of phosphoenolpyruvate mutase in high ionic strength

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0016853molecular_functionisomerase activity
A0032923biological_processorganic phosphonate biosynthetic process
A0046872molecular_functionmetal ion binding
A0050188molecular_functionphosphoenolpyruvate mutase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 300
ChainResidue
ALYS116
AARG159
AHOH453
AHOH559
AHOH561
AHOH562

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1pym
ChainResidueDetails
ALEU48
AGLY47

site_idMCSA1
Number of Residues8
DetailsM-CSA 271
ChainResidueDetails
ASER46electrostatic stabiliser, hydrogen bond donor, steric role
AGLY47electrostatic stabiliser, steric role
ALEU48electrostatic stabiliser, hydrogen bond donor, steric role
AASP85electrostatic stabiliser, hydrogen bond donor, metal ligand
AASP87electrostatic stabiliser, hydrogen bond donor
AGLU114electrostatic stabiliser, hydrogen bond donor
AARG159electrostatic stabiliser, hydrogen bond donor, promote heterolysis
AHIS190electrostatic stabiliser, hydrogen bond donor, promote heterolysis

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PDB entries from 2025-12-24

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