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3NDZ

The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0071704biological_processorganic substance metabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0071704biological_processorganic substance metabolic process
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0005975biological_processcarbohydrate metabolic process
C0071704biological_processorganic substance metabolic process
D0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
D0005975biological_processcarbohydrate metabolic process
D0071704biological_processorganic substance metabolic process
E0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
E0005975biological_processcarbohydrate metabolic process
E0030246molecular_functioncarbohydrate binding
E0030247molecular_functionpolysaccharide binding
F0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
F0005975biological_processcarbohydrate metabolic process
F0030246molecular_functioncarbohydrate binding
F0030247molecular_functionpolysaccharide binding
G0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
G0005975biological_processcarbohydrate metabolic process
G0030246molecular_functioncarbohydrate binding
G0030247molecular_functionpolysaccharide binding
H0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
H0005975biological_processcarbohydrate metabolic process
H0030246molecular_functioncarbohydrate binding
H0030247molecular_functionpolysaccharide binding
Functional Information from PROSITE/UniProt
site_idPS00659
Number of Residues10
DetailsGLYCOSYL_HYDROL_F5 Glycosyl hydrolases family 5 signature. LIFETMNEPR
ChainResidueDetails
ALEU145-ARG154

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AGLU152
BGLU152
CGLU152
DGLU152

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Nucleophile => ECO:0000250
ChainResidueDetails
AGLU275
BGLU275
CGLU275
DGLU275

221051

PDB entries from 2024-06-12

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