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1AJO

CIRCULARLY PERMUTED (1-3,1-4)-BETA-D-GLUCAN 4-GLUCANOHYDROLASE CPA16M-127

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
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 215
ChainResidue
APRO97
AGLY133
AHOH229
AHOH241
AHOH246
AASP81

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 215
ChainResidue
BASP81
BPRO97
BGLY133
BHOH244
BHOH245
BHOH257

site_idCAA
Number of Residues4
DetailsCATALYTIC SITE.
ChainResidue
ATRP191
AGLU193
AASP195
AGLU197

site_idCAB
Number of Residues4
DetailsCATALYTIC SITE.
ChainResidue
BTRP191
BGLU193
BASP195
BGLU197

Functional Information from PROSITE/UniProt
site_idPS01034
Number of Residues11
DetailsGH16_1 Glycosyl hydrolases family 16 active sites. EIDI.EflGKdT
ChainResidueDetails
AGLU193-THR203

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10064
ChainResidueDetails
AGLU193
BGLU193

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10064
ChainResidueDetails
AGLU197
BGLU197

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 2ayh
ChainResidueDetails
AASP195
AGLU193
AGLU197

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 2ayh
ChainResidueDetails
BASP195
BGLU193
BGLU197

site_idMCSA1
Number of Residues2
DetailsM-CSA 924
ChainResidueDetails
AGLU193covalent catalysis
AGLU197proton shuttle (general acid/base)

site_idMCSA2
Number of Residues2
DetailsM-CSA 924
ChainResidueDetails
BGLU193covalent catalysis
BGLU197proton shuttle (general acid/base)

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PDB entries from 2024-07-24

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