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5NR8

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

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 Residues18
Detailsbinding site for residue 95N A 401
ChainResidue
ATYR27
ATHR295
AGLU297
AMET300
AMET356
ATRP358
ALEU362
AGOL402
AGOL406
AHOH598
ATRP99
AASP138
AGLU140
AALA183
AMET210
ATYR212
AASP213
ATYR267

site_idAC2
Number of Residues7
Detailsbinding site for residue GOL A 402
ChainResidue
ATRP99
AARG269
AMET300
AARG390
AGLY391
A95N401
AHOH535

site_idAC3
Number of Residues4
Detailsbinding site for residue GOL A 403
ChainResidue
AGLN202
ALEU204
AASP205
ALYS259

site_idAC4
Number of Residues8
Detailsbinding site for residue GOL A 404
ChainResidue
ASER49
ACYS51
ATHR52
AASN87
ALEU387
APRO389
AHOH509
AHOH652

site_idAC5
Number of Residues4
Detailsbinding site for residue GOL A 405
ChainResidue
AASN30
APHE58
ATHR69
AGLU70

site_idAC6
Number of Residues7
Detailsbinding site for residue GOL A 406
ChainResidue
ATRP31
AARG35
ATHR295
AGLU297
A95N401
AHOH503
AHOH679

site_idAC7
Number of Residues9
Detailsbinding site for residue GOL A 407
ChainResidue
ATYR141
APRO185
AALA186
AMET210
ATYR212
AASP213
APHE214
AHOH505
AHOH542

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
ATYR141
AMET210
ATRP358
AGLY97
AGLU70

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

218500

PDB entries from 2024-04-17

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