9GTC
Crystal structure of human lysosomal acid-alpha-glucosidase, GAA, in complex with iminosugar compound 4g
This is a non-PDB format compatible entry.
Functional Information from PROSITE/UniProt
| site_id | PS00025 |
| Number of Residues | 22 |
| Details | P_TREFOIL_1 P-type 'Trefoil' domain signature. RfdCaPdkaiTqeqCeargCCY |
| Chain | Residue | Details |
| A | ARG89-TYR110 |
| 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 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10066","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1856189","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29061980","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29061980","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29061980","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8435067","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2016","submissionDatabase":"PDB data bank","title":"The structure of human GAA: structural basis of Pompe disease.","authors":["Deming D.T.","Garman S.C."]}},{"source":"PDB","id":"5KZW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5NN3","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"29061980","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8435067","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2016","submissionDatabase":"PDB data bank","title":"The structure of human GAA: structural basis of Pompe disease.","authors":["Deming D.T.","Garman S.C."]}},{"source":"PDB","id":"5KZW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5NN3","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29061980","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8435067","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2016","submissionDatabase":"PDB data bank","title":"The structure of human GAA: structural basis of Pompe disease.","authors":["Deming D.T.","Garman S.C."]}},{"source":"PDB","id":"5KZW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5NN3","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29061980","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8435067","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2016","submissionDatabase":"PDB data bank","title":"The structure of human GAA: structural basis of Pompe disease.","authors":["Deming D.T.","Garman S.C."]}},{"source":"PDB","id":"5KZW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5NN3","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8435067","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
