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1WNO

Crystal structure of a native chitinase from Aspergillus fumigatus YJ-407

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004568molecular_functionchitinase activity
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0006032biological_processchitin catabolic process
A0008061molecular_functionchitin binding
A0008843molecular_functionendochitinase activity
A0016787molecular_functionhydrolase activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0004568molecular_functionchitinase activity
B0005576cellular_componentextracellular region
B0005975biological_processcarbohydrate metabolic process
B0006032biological_processchitin catabolic process
B0008061molecular_functionchitin binding
B0008843molecular_functionendochitinase activity
B0016787molecular_functionhydrolase activity
Functional Information from PROSITE/UniProt
site_idPS01095
Number of Residues9
DetailsGH18_1 Glycosyl hydrolases family 18 (GH18) active site signature. FDGLDIDwE
ChainResidueDetails
APHE131-GLU139

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues728
DetailsDomain: {"description":"GH18","evidences":[{"source":"PROSITE-ProRule","id":"PRU01258","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01258","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16183021","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2A3B","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01258","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ctn
ChainResidueDetails
ATYR207
AGLU139
AASP137

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ctn
ChainResidueDetails
BTYR207
BGLU139
BASP137

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ctn
ChainResidueDetails
AGLU139
AASP137

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ctn
ChainResidueDetails
BGLU139
BASP137

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ctn
ChainResidueDetails
AASP135
AGLU139

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ctn
ChainResidueDetails
BASP135
BGLU139

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PDB entries from 2026-03-25

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