6CWZ
Crystal structure of apo SUMO E1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| C | 0004839 | molecular_function | ubiquitin activating enzyme activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0005654 | cellular_component | nucleoplasm |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0008047 | molecular_function | enzyme activator activity |
| C | 0008641 | molecular_function | ubiquitin-like modifier activating enzyme activity |
| C | 0016567 | biological_process | protein ubiquitination |
| C | 0016874 | molecular_function | ligase activity |
| C | 0016925 | biological_process | protein sumoylation |
| C | 0019948 | molecular_function | SUMO activating enzyme activity |
| C | 0031510 | cellular_component | SUMO activating enzyme complex |
| C | 0033235 | biological_process | positive regulation of protein sumoylation |
| C | 0036211 | biological_process | protein modification process |
| C | 0043008 | molecular_function | ATP-dependent protein binding |
| C | 0044388 | molecular_function | small protein activating enzyme binding |
| C | 0046982 | molecular_function | protein heterodimerization activity |
| C | 1903955 | biological_process | positive regulation of protein targeting to mitochondrion |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0005515 | molecular_function | protein binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005634 | cellular_component | nucleus |
| D | 0005654 | cellular_component | nucleoplasm |
| D | 0005730 | cellular_component | nucleolus |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0008641 | molecular_function | ubiquitin-like modifier activating enzyme activity |
| D | 0016740 | molecular_function | transferase activity |
| D | 0016925 | biological_process | protein sumoylation |
| D | 0019948 | molecular_function | SUMO activating enzyme activity |
| D | 0031510 | cellular_component | SUMO activating enzyme complex |
| D | 0032183 | molecular_function | SUMO binding |
| D | 0033235 | biological_process | positive regulation of protein sumoylation |
| D | 0044388 | molecular_function | small protein activating enzyme binding |
| D | 0044390 | molecular_function | ubiquitin-like protein conjugating enzyme binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0046982 | molecular_function | protein heterodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN D 701 |
| Chain | Residue |
| D | CYS158 |
| D | CYS161 |
| D | CYS441 |
| D | CYS444 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10132","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15660128","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20164921","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15660128","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 3 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate"} |
| Chain | Residue | Details |
