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6I6X

New Irreversible a-l-Iduronidase Inhibitors and Activity-Based Probes

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
Functional Information from PROSITE/UniProt
site_idPS01027
Number of Residues10
DetailsGLYCOSYL_HYDROL_F39 Glycosyl hydrolases family 39 active site. WnFEtWNEPD
ChainResidueDetails
BTRP175-ASP184
ATRP175-ASP184

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10068, ECO:0000269|PubMed:24036510
ChainResidueDetails
BGLU182

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:24036510
ChainResidueDetails
BGLU299

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:23959878, ECO:0000269|PubMed:24036510, ECO:0007744|PDB:3W81, ECO:0007744|PDB:3W82, ECO:0007744|PDB:4KGL
ChainResidueDetails
BPRO54
BLEU56
BHIS58

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:23959878, ECO:0007744|PDB:3W82
ChainResidueDetails
BHIS91
BASN181
BGLU182
BLYS264
BGLU299
BGLY305
BASP349
BARG363

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:23959878, ECO:0000269|PubMed:24036510, ECO:0007744|PDB:3W81, ECO:0007744|PDB:3W82, ECO:0007744|PDB:4KGJ, ECO:0007744|PDB:4KH2
ChainResidueDetails
BTRP306

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:23959878, ECO:0007744|PDB:3W81, ECO:0007744|PDB:3W82
ChainResidueDetails
BARG488
BARG492

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:23959878, ECO:0000269|PubMed:24036510, ECO:0007744|PDB:3W81, ECO:0007744|PDB:3W82, ECO:0007744|PDB:4KGJ, ECO:0007744|PDB:4KGL, ECO:0007744|PDB:4KH2, ECO:0007744|PDB:4MJ2, ECO:0007744|PDB:4MJ4
ChainResidueDetails
BASN110

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23959878, ECO:0007744|PDB:3W81, ECO:0007744|PDB:3W82
ChainResidueDetails
BASN190

site_idSWS_FT_FI9
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
BASN336

site_idSWS_FT_FI10
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23959878, ECO:0000269|PubMed:24036510, ECO:0007744|PDB:3W81, ECO:0007744|PDB:3W82, ECO:0007744|PDB:4KGJ, ECO:0007744|PDB:4KGL, ECO:0007744|PDB:4KH2, ECO:0007744|PDB:4MJ2, ECO:0007744|PDB:4MJ4
ChainResidueDetails
BASN372
BASN415

site_idSWS_FT_FI11
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23959878, ECO:0007744|PDB:3W81
ChainResidueDetails
BASN451

223166

PDB entries from 2024-07-31

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