3HY2
Crystal Structure of Sulfiredoxin in Complex with Peroxiredoxin I and ATP:Mg2+
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001501 | biological_process | skeletal system development |
| A | 0003723 | molecular_function | RNA binding |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0008283 | biological_process | cell population proliferation |
| A | 0008379 | molecular_function | thioredoxin peroxidase activity |
| A | 0016209 | molecular_function | antioxidant activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019430 | biological_process | removal of superoxide radicals |
| A | 0030101 | biological_process | natural killer cell activation |
| A | 0042470 | cellular_component | melanosome |
| A | 0042744 | biological_process | hydrogen peroxide catabolic process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0045296 | molecular_function | cadherin binding |
| A | 0045321 | biological_process | leukocyte activation |
| A | 0045454 | biological_process | cell redox homeostasis |
| A | 0051920 | molecular_function | peroxiredoxin activity |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0140824 | molecular_function | thioredoxin-dependent peroxiredoxin activity |
| B | 0001501 | biological_process | skeletal system development |
| B | 0003723 | molecular_function | RNA binding |
| B | 0004601 | molecular_function | peroxidase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005615 | cellular_component | extracellular space |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006979 | biological_process | response to oxidative stress |
| B | 0008283 | biological_process | cell population proliferation |
| B | 0008379 | molecular_function | thioredoxin peroxidase activity |
| B | 0016209 | molecular_function | antioxidant activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019430 | biological_process | removal of superoxide radicals |
| B | 0030101 | biological_process | natural killer cell activation |
| B | 0042470 | cellular_component | melanosome |
| B | 0042744 | biological_process | hydrogen peroxide catabolic process |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0045296 | molecular_function | cadherin binding |
| B | 0045321 | biological_process | leukocyte activation |
| B | 0045454 | biological_process | cell redox homeostasis |
| B | 0051920 | molecular_function | peroxiredoxin activity |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0140824 | molecular_function | thioredoxin-dependent peroxiredoxin activity |
| X | 0032542 | molecular_function | sulfiredoxin activity |
| Y | 0032542 | molecular_function | sulfiredoxin activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ATP X 1 |
| Chain | Residue |
| A | ASP52 |
| X | THR68 |
| X | SER75 |
| X | PRO77 |
| X | GLY98 |
| X | ALA99 |
| X | HIS100 |
| X | ARG101 |
| X | HOH140 |
| X | HOH176 |
| X | HOH217 |
| A | LYS93 |
| X | HOH318 |
| A | MG207 |
| A | HOH245 |
| A | HOH248 |
| A | HOH275 |
| X | LYS61 |
| X | SER64 |
| X | LEU65 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ATP Y 2 |
| Chain | Residue |
| B | ASP52 |
| B | LYS93 |
| B | MG207 |
| B | HOH275 |
| B | HOH282 |
| B | HOH315 |
| Y | LYS61 |
| Y | SER64 |
| Y | LEU65 |
| Y | THR68 |
| Y | SER75 |
| Y | PRO77 |
| Y | GLY98 |
| Y | ALA99 |
| Y | HIS100 |
| Y | ARG101 |
| Y | HOH138 |
| Y | HOH207 |
| Y | HOH242 |
| Y | HOH254 |
| Y | HOH293 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 207 |
| Chain | Residue |
| A | ASP52 |
| A | HOH245 |
| A | HOH248 |
| X | ATP1 |
| X | HOH140 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 207 |
| Chain | Residue |
| B | ASP52 |
| B | HOH275 |
| B | HOH282 |
| Y | ATP2 |
| Y | HOH138 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 318 |
| Details | Domain: {"description":"Thioredoxin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00691","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Cysteine sulfenic acid (-SOH) intermediate","evidences":[{"source":"PubMed","id":"12059788","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"12161445","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P35700","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine; by CDK1","evidences":[{"source":"PubMed","id":"11986303","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P35700","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| 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_FI10 |
| Number of Residues | 4 |
| 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_FI11 |
| Number of Residues | 2 |
| 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_FI12 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15952770","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
