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1GUV

Structure of human chitotriosidase

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 Residues5
DetailsBINDING SITE FOR RESIDUE EDO A1388
ChainResidue
AVAL281
AGLN317
AARG318
ATYR326
AHOH2258

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A1389
ChainResidue
AGLU176
AARG177
ALEU179

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A1390
ChainResidue
AVAL150
AARG154
AALA111

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A1391
ChainResidue
AALA22
ALEU387
AHOH2002
AHOH2251

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A1392
ChainResidue
AGLY289
ATHR290
ALEU301
ATRP309
AGLN332
AHOH2203
AHOH2224

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A1393
ChainResidue
ALYS23
AEDO1397
AHOH2004
AHOH2187

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A1394
ChainResidue
ASER122
AARG125
APHE126
ALYS129
AHOH2119

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A1395
ChainResidue
ATRP71
APRO88
AHOH2262
AHOH2263

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A1396
ChainResidue
ALYS44
AGLU79
AHOH2265

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A1397
ChainResidue
ALYS23
AASP205
AEDO1393
AHOH2267
AHOH2268
AHOH2269
AHOH2270

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

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ctn
ChainResidueDetails
ATYR212
AASP138
AGLU140

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ctn
ChainResidueDetails
AASP138
AGLU140

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ctn
ChainResidueDetails
AASP136
AGLU140

246031

PDB entries from 2025-12-10

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