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2EXO

CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF THE BETA-1,4-GLYCANASE CEX FROM CELLULOMONAS FIMI

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
Functional Information from PROSITE/UniProt
site_idPS00591
Number of Residues11
DetailsGH10_1 Glycosyl hydrolases family 10 (GH10) active site. GVDVrITELDI
ChainResidueDetails
AGLY226-ILE236

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues310
DetailsDomain: {"description":"GH10","evidences":[{"source":"PROSITE-ProRule","id":"PRU01096","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"7918478","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10061","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1678739","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1exp
ChainResidueDetails
AGLU127
AGLU233
AASP235
AHIS205

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1exp
ChainResidueDetails
AGLU127

site_idMCSA1
Number of Residues5
DetailsM-CSA 548
ChainResidueDetails
AGLU127proton acceptor, proton donor
AASN169electrostatic stabiliser
AHIS205electrostatic stabiliser
AGLU233electrostatic stabiliser, nucleofuge, nucleophile
AASP235electrostatic stabiliser

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PDB entries from 2025-07-30

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