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6JK6

Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound 2-8-s2

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0008061molecular_functionchitin binding
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue BV0 A 501
ChainResidue
ATRP99
AGLY373
ABV0502
AHOH610
AHOH622
AHOH647
AHOH745
AHOH751
AASP138
AGLU140
ATYR141
ATYR190
AMET210
ATYR212
AGLU297
ATRP358

site_idAC2
Number of Residues5
Detailsbinding site for residue BV0 A 502
ChainResidue
ATYR190
AASP213
ATRP218
AASN371
ABV0501

Functional Information from PROSITE/UniProt
site_idPS01095
Number of Residues9
DetailsGH18_1 Glycosyl hydrolases family 18 (GH18) active site signature. FDGLDLDwE
ChainResidueDetails
APHE132-GLU140

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01258","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01258","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; in variant S-102","evidences":[{"source":"PubMed","id":"19725875","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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