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1CTN

CRYSTAL STRUCTURE OF A BACTERIAL CHITINASE AT 2.3 ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004568molecular_functionchitinase activity
A0005975biological_processcarbohydrate metabolic process
A0006032biological_processchitin catabolic process
A0008061molecular_functionchitin binding
A0008843molecular_functionendochitinase activity
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
Functional Information from PDB Data
site_idCA
Number of Residues2
Details
ChainResidue
AGLU315
AASP391

Functional Information from PROSITE/UniProt
site_idPS01095
Number of Residues9
DetailsGH18_1 Glycosyl hydrolases family 18 (GH18) active site signature. FDGVDIDwE
ChainResidueDetails
APHE307-GLU315

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues401
DetailsDomain: {"description":"GH18","evidences":[{"source":"PROSITE-ProRule","id":"PRU01258","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01258","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 12369923, 11560481, 11846790
ChainResidueDetails
AGLU315

site_idMCSA1
Number of Residues4
DetailsM-CSA 478
ChainResidueDetails
AASP311electrostatic stabiliser
AASP313steric role
AGLU315proton shuttle (general acid/base)
ATYR390electrostatic destabiliser

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PDB entries from 2025-12-24

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