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Search The CSA
PDB ID
UNIPROT ID
EC Number

Catalytic Site Atlas

CSA LITERATURE entry for 1bgl

E.C. namebeta-galactosidase
SpeciesEscherichia coli (Bacteria)
E.C. Number (IntEnz) 3.2.1.23
CSA Homologues of 1bglThere are 52 Homologs
CSA Entries With UniProtID P00722
CSA Entries With EC Number 3.2.1.23
PDBe Entry 1bgl
PDBSum Entry 1bgl
MACiE Entry 1bgl

Literature Report

Introduction
Mechansim
Reaction

Catalytic Sites for 1bgl

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluA461462macie:sideChain
GluA537538macie:sideChain

Annotated By Reference To The Literature - Site 2 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluB461462macie:sideChain
GluB537538macie:sideChain

Annotated By Reference To The Literature - Site 3 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluC461462macie:sideChain
GluC537538macie:sideChain

Annotated By Reference To The Literature - Site 4 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluD461462macie:sideChain
GluD537538macie:sideChain

Annotated By Reference To The Literature - Site 5 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluE461462macie:sideChain
GluE537538macie:sideChain

Annotated By Reference To The Literature - Site 6 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluF461462macie:sideChain
GluF537538macie:sideChain

Annotated By Reference To The Literature - Site 7 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluG461462macie:sideChain
GluG537538macie:sideChain

Annotated By Reference To The Literature - Site 8 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluH461462macie:sideChain
GluH537538macie:sideChain

Literature References

Notes:
Davies G
Structures and mechanisms of glycosyl hydrolases.
Structure 1995 3 853-859
PubMed: 8535779
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