Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5HBF

Crystal structure of human full-length chitotriosidase (CHIT1)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0008061molecular_functionchitin binding
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005576cellular_componentextracellular region
B0005975biological_processcarbohydrate metabolic process
B0008061molecular_functionchitin binding
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue GOL A 501
ChainResidue
ATYR141
APRO185
AALA186
AGLY187
ATYR190
AMET210
ATYR212
AASP213
AARG470

site_idAC2
Number of Residues6
Detailsbinding site for residue GOL A 502
ChainResidue
ATYR303
ALYS314
AASP336
AVAL337
AGLN372
AHOH662

site_idAC3
Number of Residues3
Detailsbinding site for residue GOL B 501
ChainResidue
BTRP31
BASN100
BLEU473

site_idAC4
Number of Residues7
Detailsbinding site for residue GOL B 502
ChainResidue
BTRP99
BASP213
BTYR267
BARG269
BTRP358
BARG470
BHOH640

Functional Information from PROSITE/UniProt
site_idPS00028
Number of Residues21
DetailsZINC_FINGER_C2H2_1 Zinc finger C2H2 type domain signature. Ckc..CtwnLvprgslehHhhh..H
ChainResidueDetails
ACYS460-HIS480

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 Residues49
DetailsDomain: {"description":"Chitin-binding type-2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00144","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01258","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01258","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; in variant S-102","evidences":[{"source":"PubMed","id":"19725875","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

PDB statisticsPDBj update infoContact PDBjnumon