4WKA

Crystal structure of human chitotriosidase-1 catalytic domain at 0.95 A resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0005975	biological_process	carbohydrate metabolic process
A	0008061	molecular_function	chitin binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	binding site for residue TLA A 401

Chain	Residue
A	VAL110
A	HOH923
A	HOH1049
A	ALA111
A	THR112
A	ARG116
A	ARG154
A	HOH525
A	HOH534
A	HOH820
A	HOH837

---

site_id	AC2
Number of Residues	9
Details	binding site for residue TLA A 402

Chain	Residue
A	SER308
A	SER308
A	TRP309
A	TRP309
A	LYS310
A	LYS310
A	ARG327
A	ARG327
A	HOH540

---

Functional Information from PROSITE/UniProt

site_id	PS01095
Number of Residues	9
Details	GH18_1 Glycosyl hydrolases family 18 (GH18) active site signature. FDGLDLDwE

Chain	Residue	Details
A	PHE132-GLU140

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01258","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01258","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; in variant S-102","evidences":[{"source":"PubMed","id":"19725875","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---