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3LB9

Crystal structure of the B. circulans cpA123 circular permutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0005975biological_processcarbohydrate metabolic process
Functional Information from PROSITE/UniProt
site_idPS00776
Number of Residues11
DetailsGH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PLiEYYVVDsW
ChainResidueDetails
APRO140-TRP150

site_idPS00777
Number of Residues12
DetailsGH11_2 Glycosyl hydrolases family 11 (GH11) active site signature 2. MatEGYQSSGsS
ChainResidueDetails
AMET48-SER59

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10062, ECO:0000269|PubMed:8019418
ChainResidueDetails
AGLU143
BGLU143
CGLU143

site_idSWS_FT_FI2
Number of Residues3
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10063, ECO:0000269|PubMed:8019418
ChainResidueDetails
AGLU51
BGLU51
CGLU51

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 432
ChainResidueDetails
AGLU51proton shuttle (general acid/base)
AASN100modifies pKa
ATYR134electrostatic destabiliser
AGLU143covalent catalysis, proton shuttle (general acid/base)
ATYR145modifies pKa

site_idMCSA2
Number of Residues5
DetailsM-CSA 432
ChainResidueDetails
BGLU51proton shuttle (general acid/base)
BASN100modifies pKa
BTYR134electrostatic destabiliser
BGLU143covalent catalysis, proton shuttle (general acid/base)
BTYR145modifies pKa

site_idMCSA3
Number of Residues5
DetailsM-CSA 432
ChainResidueDetails
CGLU51proton shuttle (general acid/base)
CASN100modifies pKa
CTYR134electrostatic destabiliser
CGLU143covalent catalysis, proton shuttle (general acid/base)
CTYR145modifies pKa

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PDB entries from 2024-07-24

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