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1VRX

Endocellulase e1 from acidothermus cellulolyticus mutant y245g

Replaces:  1C0D
Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
B0000272biological_processpolysaccharide catabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
Functional Information from PROSITE/UniProt
site_idPS00659
Number of Residues10
DetailsGLYCOSYL_HYDROL_F5 Glycosyl hydrolases family 5 signature. VGFDLHNEPH
ChainResidueDetails
AVAL155-HIS164

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor
ChainResidueDetails
AGLU162
BGLU162

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile
ChainResidueDetails
AGLU282
BGLU282

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1bqc
ChainResidueDetails
AHIS238
AASN161
ATYR240
AGLU282
AGLU162

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1bqc
ChainResidueDetails
BHIS238
BASN161
BTYR240
BGLU282
BGLU162

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1bqc
ChainResidueDetails
AARG62
AGLU282
AGLU162

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1bqc
ChainResidueDetails
BARG62
BGLU282
BGLU162

226707

PDB entries from 2024-10-30

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