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9B87

Tetrameric cryo-EM structure of E. coli BcsZ

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0005576cellular_componentextracellular region
A0008810molecular_functioncellulase activity
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030245biological_processcellulose catabolic process
B0000272biological_processpolysaccharide catabolic process
B0005576cellular_componentextracellular region
B0008810molecular_functioncellulase activity
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0030245biological_processcellulose catabolic process
C0000272biological_processpolysaccharide catabolic process
C0005576cellular_componentextracellular region
C0008810molecular_functioncellulase activity
C0016787molecular_functionhydrolase activity
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0030245biological_processcellulose catabolic process
D0000272biological_processpolysaccharide catabolic process
D0005576cellular_componentextracellular region
D0008810molecular_functioncellulase activity
D0016787molecular_functionhydrolase activity
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0030245biological_processcellulose catabolic process
Functional Information from PROSITE/UniProt
site_idPS00812
Number of Residues19
DetailsGLYCOSYL_HYDROL_F8 Glycosyl hydrolases family 8 signature. ASDGDvwMAwSLLeAgrlW
ChainResidueDetails
AALA114-TRP132

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10058","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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