spacer
View the latest EBI news stories and important announcements...
more

spacer
Search The CSA
PDB ID
UNIPROT ID
EC Number

Catalytic Site Atlas

CSA LITERATURE entry for 1xva

E.C. nameglycine N-methyltransferase
SpeciesEscherichia coli (Bacteria)
E.C. Number (IntEnz) 2.1.1.20
CSA Homologues of 1xvaThere are 12 Homologs
CSA Entries With UniProtID P13255
CSA Entries With EC Number 2.1.1.20
PDBe Entry 1xva
PDBSum Entry 1xva
MACiE Entry M0023

Literature Report

Introduction
Mechansim
Reaction

Catalytic Sites for 1xva

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
TyrA21macie:sideChainTyr21 forms an electrostatic interaction with the S+ of SAM, stabilising the transition state.
GlyA137macie:mainChainCarbonylGly137 forms a hydrogen bond to the amine group of glycine. This bond strengthens upon moving to the transition state, thus stabilising it.
TyrA194macie:sideChainTyr242 forms a hydrogen bond to the amine group of glycine. This bond strengthens upon moving to the transition state, thus stabilising it
ArgA175macie:sideChainArg175 is selective for the basic form of glycine (amine group neutral and carboxylic group deprotonated) over the zwitterionic tautomer. This provides better stabilisation of the transition state.
HisA142macie:sideChainHis142 accepts a hydrogen bond from the hydroxyl group of Tyr21, freeing up the lone pair of Tyr21 to stabilise the S+ of SAM

Annotated By Reference To The Literature - Site 2 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GlyB137macie:mainChainCarbonylGly137 forms a hydrogen bond to the amine group of glycine. This bond strengthens upon moving to the transition state, thus stabilising it.
ArgB175macie:sideChainArg175 is selective for the basic form of glycine (amine group neutral and carboxylic group deprotonated) over the zwitterionic tautomer. This provides better stabilisation of the transition state.
TyrB194macie:sideChainTyr242 forms a hydrogen bond to the amine group of glycine. This bond strengthens upon moving to the transition state, thus stabilising it
TyrB21macie:sideChainTyr21 forms an electrostatic interaction with the S+ of SAM, stabilising the transition state.
HisB142macie:sideChainHis142 accepts a hydrogen bond from the hydroxyl group of Tyr21, freeing up the lone pair of Tyr21 to stabilise the S+ of SAM

Literature References

Notes:
Fu Z
Crystal structure of glycine N-methyltransferase from rat liver.
Biochemistry 1996 35 11985-11993
PubMed: 8810903
spacer
spacer