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1EDG

SINGLE CRYSTAL STRUCTURE DETERMINATION OF THE CATALYTIC DOMAIN OF CELCCA CARRIED OUT AT 15 DEGREE C

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
Functional Information from PROSITE/UniProt
site_idPS00659
Number of Residues10
DetailsGLYCOSYL_HYDROL_F5 Glycosyl hydrolases family 5 signature. LIFEGMNEPR
ChainResidueDetails
ALEU163-ARG172

site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. AGLAmaDgGTNAWNI
ChainResidueDetails
AALA262-ILE276

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000305
ChainResidueDetails
AHIS122

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor
ChainResidueDetails
AGLU170

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Nucleophile
ChainResidueDetails
AGLU307

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1bqc
ChainResidueDetails
AHIS254
AGLU170
AASN169
ATYR256
AGLU307

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PDB entries from 2024-07-24

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