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1LQ0

CRYSTAL STRUCTURE OF HUMAN CHITOTRIOSIDASE AT 2.2 ANGSTROM RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0008061molecular_functionchitin binding
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
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01258
ChainResidueDetails
AGLU140

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01258
ChainResidueDetails
AGLU70
AGLY97
ATYR141
AMET210
ATRP358

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; in variant S-102 => ECO:0000269|PubMed:19725875
ChainResidueDetails
AASN100

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

227344

PDB entries from 2024-11-13

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