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3MMW

Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004338molecular_functionglucan exo-1,3-beta-glucosidase activity
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0009251biological_processglucan catabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0000272biological_processpolysaccharide catabolic process
B0004338molecular_functionglucan exo-1,3-beta-glucosidase activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0009251biological_processglucan catabolic process
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0000272biological_processpolysaccharide catabolic process
C0004338molecular_functionglucan exo-1,3-beta-glucosidase activity
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0005975biological_processcarbohydrate metabolic process
C0009251biological_processglucan catabolic process
C0016787molecular_functionhydrolase activity
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0000272biological_processpolysaccharide catabolic process
D0004338molecular_functionglucan exo-1,3-beta-glucosidase activity
D0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
D0005975biological_processcarbohydrate metabolic process
D0009251biological_processglucan catabolic process
D0016787molecular_functionhydrolase activity
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 318
ChainResidue
AHIS96
AGLU98
AHOH321
AHOH323

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 319
ChainResidue
AGLU99
AHOH324
BGLU99
BHOH324

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CD A 320
ChainResidue
AGLU253
AHOH328
AHOH369
AHOH399
AHOH703
AHOH994
AGLU136

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CD B 318
ChainResidue
BHIS96
BGLU98
BHOH320
BHOH322
BHOH671

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CD B 319
ChainResidue
BGLU136
BGLU253
BHOH367
BHOH413
BHOH533

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD C 318
ChainResidue
CHIS96
CGLU98
CHOH322
DHOH991

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CD C 319
ChainResidue
CGLU99
CHOH328
DGLU99

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CD C 320
ChainResidue
CGLU136
CGLU253
CHOH327
CHOH330
CHOH331
CHOH332

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CD C 321
ChainResidue
CGLU78
CHOH334
CHOH355

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD D 318
ChainResidue
CHOH326
DHIS96
DGLU98
DHOH321

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CD D 319
ChainResidue
DGLU136
DGLU253
DHOH323
DHOH399
DHOH499
DHOH992

Functional Information from PROSITE/UniProt
site_idPS00659
Number of Residues10
DetailsGLYCOSYL_HYDROL_F5 Glycosyl hydrolases family 5 signature. LFFEILNEPH
ChainResidueDetails
ALEU129-HIS138

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PDB entries from 2025-12-03

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