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1EGZ

CELLULASE CEL5 FROM ERWINIA CHRYSANTHEMI, A FAMILY GH 5-2 ENZYME

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
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 300
ChainResidue
AASN161
AHOH1348
AHOH1401
AGLY121
AASP158
AASP160

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 300
ChainResidue
BGLY121
BASP158
BASP160
BASN161
BHOH2336

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 300
ChainResidue
CGLY121
CASP158
CASP160
CASN161
CHOH3345
CHOH3383

site_idCTA
Number of Residues2
DetailsGLU133 IS THE NUCLEOPHILE AND GLU220 THE ACID/BASE AT THE CATALYTIC SITE OF THIS GLYCOSYL HYDROLASE
ChainResidue
AGLU133
AGLU220

site_idCTB
Number of Residues2
DetailsGLU133 IS THE NUCLEOPHILE AND GLU220 THE ACID/BASE AT THE CATALYTIC SITE OF THIS GLYCOSYL HYDROLASE
ChainResidue
BGLU133
BGLU220

site_idCTC
Number of Residues2
DetailsGLU133 IS THE NUCLEOPHILE AND GLU220 THE ACID/BASE AT THE CATALYTIC SITE OF THIS GLYCOSYL HYDROLASE
ChainResidue
CGLU133
CGLU220

Functional Information from PROSITE/UniProt
site_idPS00659
Number of Residues10
DetailsGLYCOSYL_HYDROL_F5 Glycosyl hydrolases family 5 signature. VIYEIYNEPL
ChainResidueDetails
AVAL126-LEU135

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Proton donor
ChainResidueDetails
AGLU133
BGLU133
CGLU133

site_idSWS_FT_FI2
Number of Residues3
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:O85465
ChainResidueDetails
AGLU220
BGLU220
CGLU220

220472

PDB entries from 2024-05-29

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