8CB1
Crystal structure of human lysosomal acid-alpha-glucosidase, GAA, in complex with N-PNT-DNM 15
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0030246 | molecular_function | carbohydrate binding |
| G | 0003824 | molecular_function | catalytic activity |
| G | 0005975 | biological_process | carbohydrate metabolic process |
| G | 0030246 | molecular_function | carbohydrate binding |
Functional Information from PROSITE/UniProt
| site_id | PS00129 |
| Number of Residues | 8 |
| Details | GLYCOSYL_HYDROL_F31_1 Glycosyl hydrolases family 31 active site. GMWiDMNE |
| Chain | Residue | Details |
| A | GLY514-GLU521 |
| site_id | PS00707 |
| Number of Residues | 31 |
| Details | GLYCOSYL_HYDROL_F31_2 Glycosyl hydrolases family 31 signature 2. GADVCGFlgnTseeLCvRWtqLGAFyPFmRN |
| Chain | Residue | Details |
| A | GLY643-ASN673 |
| site_id | PS00025 |
| Number of Residues | 22 |
| Details | P_TREFOIL_1 P-type 'Trefoil' domain signature. RfdCaPdkaiTqeqCeargCCY |
| Chain | Residue | Details |
| G | ARG89-TYR110 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10066, ECO:0000269|PubMed:1856189, ECO:0000305|PubMed:29061980 |
| Chain | Residue | Details |
| A | ASP518 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250 |
| Chain | Residue | Details |
| A | GLU521 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:29061980 |
| Chain | Residue | Details |
| A | ASP404 | |
| A | ARG600 | |
| A | ASP616 | |
| A | HIS674 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:29061980, ECO:0000269|PubMed:8435067, ECO:0000269|Ref.19, ECO:0007744|PDB:5KZW, ECO:0007744|PDB:5NN3 |
| Chain | Residue | Details |
| A | ASN233 | |
| A | ASN652 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:29061980, ECO:0000269|PubMed:8435067, ECO:0000269|Ref.19, ECO:0007744|PDB:5KZW, ECO:0007744|PDB:5NN3 |
| Chain | Residue | Details |
| A | ASN390 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:29061980, ECO:0000269|PubMed:8435067, ECO:0000269|Ref.19, ECO:0007744|PDB:5KZW, ECO:0007744|PDB:5NN3 |
| Chain | Residue | Details |
| A | ASN470 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:29061980, ECO:0000269|PubMed:8435067, ECO:0000269|Ref.19, ECO:0007744|PDB:5KZW, ECO:0007744|PDB:5NN3 |
| Chain | Residue | Details |
| A | ASN882 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:8435067 |
| Chain | Residue | Details |
| A | ASN925 |
