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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 1cb7

E.C. namemethylaspartate mutase
SpeciesClostridium cochlearium (Bacteria)
E.C. Number (IntEnz) 5.4.99.1
CSA Homologues of 1cb7There are 10 Homologs
CSA Entries With UniProtID P80077
CSA Entries With EC Number 5.4.99.1
PDBe Entry 1cb7
PDBSum Entry 1cb7
MACiE Entry M0063

Literature Report

Introduction
Mechansim
Reaction

Catalytic Sites for 1cb7

Annotated By Reference To The Literature - Site 3 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluB171171macie:sideChain

Annotated By Reference To The Literature - Site 4 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluD171171macie:sideChain

Literature References

Notes:
Reitzer R
Glutamate mutase from Clostridium cochlearium: the structure of a coenzyme B12-dependent enzyme provides new mechanistic insights.
Structure 1999 7 891-902
PubMed: 10467146
Madhavapeddi P
The role of the active site glutamate in the rearrangement of glutamate to 3-methylaspartate catalyzed by adenosylcobalamin-dependent glutamate mutase.
Chem Biol 2001 8 1143-1149
PubMed: 11755393
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