7SCH
Cryo-EM structure of the human Exostosin-1 and Exostosin-2 heterodimer
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000139 | cellular_component | Golgi membrane |
| A | 0000271 | biological_process | polysaccharide biosynthetic process |
| A | 0001503 | biological_process | ossification |
| A | 0005515 | molecular_function | protein binding |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0005794 | cellular_component | Golgi apparatus |
| A | 0006024 | biological_process | glycosaminoglycan biosynthetic process |
| A | 0006486 | biological_process | obsolete protein glycosylation |
| A | 0008375 | molecular_function | acetylglucosaminyltransferase activity |
| A | 0009101 | biological_process | glycoprotein biosynthetic process |
| A | 0015012 | biological_process | heparan sulfate proteoglycan biosynthetic process |
| A | 0015020 | molecular_function | glucuronosyltransferase activity |
| A | 0016020 | cellular_component | membrane |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0031090 | cellular_component | organelle membrane |
| A | 0042328 | molecular_function | heparan sulfate N-acetylglucosaminyltransferase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0046982 | molecular_function | protein heterodimerization activity |
| A | 0050508 | molecular_function | glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity |
| A | 0050509 | molecular_function | N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity |
| A | 1902494 | cellular_component | catalytic complex |
| B | 0000139 | cellular_component | Golgi membrane |
| B | 0000271 | biological_process | polysaccharide biosynthetic process |
| B | 0001503 | biological_process | ossification |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005789 | cellular_component | endoplasmic reticulum membrane |
| B | 0005794 | cellular_component | Golgi apparatus |
| B | 0006024 | biological_process | glycosaminoglycan biosynthetic process |
| B | 0006486 | biological_process | obsolete protein glycosylation |
| B | 0008375 | molecular_function | acetylglucosaminyltransferase activity |
| B | 0009101 | biological_process | glycoprotein biosynthetic process |
| B | 0015012 | biological_process | heparan sulfate proteoglycan biosynthetic process |
| B | 0015020 | molecular_function | glucuronosyltransferase activity |
| B | 0016020 | cellular_component | membrane |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0042328 | molecular_function | heparan sulfate N-acetylglucosaminyltransferase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0043541 | cellular_component | UDP-N-acetylglucosamine transferase complex |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0046982 | molecular_function | protein heterodimerization activity |
| B | 0050508 | molecular_function | glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity |
| B | 0050509 | molecular_function | N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 1902494 | cellular_component | catalytic complex |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"36593275","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7SCJ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"36593275","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7SCJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7SCK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7UQY","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"36593275","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7SCJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7SCK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7UQX","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"36402845","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36593275","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7SCJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7SCK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7UQX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7UQY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7ZAY","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"36402845","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7ZAY","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"36402845","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36593275","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7SCK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7ZAY","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"36402845","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36593275","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7SCK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7UQY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7ZAY","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"36402845","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7ZAY","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9ES89","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"36593275","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7SCK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"36402845","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36593275","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7SCH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7SCJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7SCK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7UQX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7UQY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7ZAY","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
