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5NRF

Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound 7i

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 Residues19
Detailsbinding site for residue 95Q A 401
ChainResidue
ATYR27
AARG269
ATHR295
AGLU297
AMET300
AMET356
ATRP358
ALEU362
AARG390
AGLY391
AHOH503
ATRP99
AASP138
AGLU140
AALA183
AMET210
ATYR212
AASP213
ATYR267

site_idAC2
Number of Residues8
Detailsbinding site for residue GOL A 402
ChainResidue
ATYR141
APRO185
AALA186
AGLY187
AMET210
ATYR212
AASP213
AHOH501

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

244693

PDB entries from 2025-11-12

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