5NN5
Crystal structure of human lysosomal acid-alpha-glucosidase, GAA, in complex with 1-deoxynojirimycin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000023 | biological_process | maltose metabolic process |
| A | 0002026 | biological_process | regulation of the force of heart contraction |
| A | 0002086 | biological_process | diaphragm contraction |
| A | 0003007 | biological_process | heart morphogenesis |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0004558 | molecular_function | alpha-1,4-glucosidase activity |
| A | 0005764 | cellular_component | lysosome |
| A | 0005765 | cellular_component | lysosomal membrane |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0005977 | biological_process | glycogen metabolic process |
| A | 0005980 | biological_process | glycogen catabolic process |
| A | 0005984 | biological_process | disaccharide metabolic process |
| A | 0005985 | biological_process | sucrose metabolic process |
| A | 0006006 | biological_process | glucose metabolic process |
| A | 0006941 | biological_process | striated muscle contraction |
| A | 0007040 | biological_process | lysosome organization |
| A | 0007626 | biological_process | locomotory behavior |
| A | 0009888 | biological_process | tissue development |
| A | 0016020 | cellular_component | membrane |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0030246 | molecular_function | carbohydrate binding |
| A | 0035577 | cellular_component | azurophil granule membrane |
| A | 0035904 | biological_process | aorta development |
| A | 0043181 | biological_process | vacuolar sequestering |
| A | 0043202 | cellular_component | lysosomal lumen |
| A | 0046716 | biological_process | muscle cell cellular homeostasis |
| A | 0050884 | biological_process | neuromuscular process controlling posture |
| A | 0050885 | biological_process | neuromuscular process controlling balance |
| A | 0060048 | biological_process | cardiac muscle contraction |
| A | 0061723 | biological_process | glycophagy |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0070821 | cellular_component | tertiary granule membrane |
| A | 0090599 | molecular_function | alpha-glucosidase activity |
| A | 0101003 | cellular_component | ficolin-1-rich granule membrane |
| A | 0120282 | cellular_component | autolysosome lumen |
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 |
