1QQ2
CRYSTAL STRUCTURE OF A MAMMALIAN 2-CYS PEROXIREDOXIN, HBP23.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000302 | biological_process | response to reactive oxygen species |
| A | 0000791 | cellular_component | euchromatin |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0005782 | cellular_component | peroxisomal matrix |
| 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 | 0020037 | molecular_function | heme binding |
| A | 0030101 | biological_process | natural killer cell activation |
| A | 0032872 | biological_process | regulation of stress-activated MAPK cascade |
| A | 0034101 | biological_process | erythrocyte homeostasis |
| A | 0042267 | biological_process | natural killer cell mediated cytotoxicity |
| A | 0042744 | biological_process | hydrogen peroxide catabolic process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0045321 | biological_process | leukocyte activation |
| A | 0045454 | biological_process | cell redox homeostasis |
| A | 0051920 | molecular_function | peroxiredoxin activity |
| A | 0140824 | molecular_function | thioredoxin-dependent peroxiredoxin activity |
| B | 0000302 | biological_process | response to reactive oxygen species |
| B | 0000791 | cellular_component | euchromatin |
| B | 0004601 | molecular_function | peroxidase activity |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0005782 | cellular_component | peroxisomal matrix |
| 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 | 0020037 | molecular_function | heme binding |
| B | 0030101 | biological_process | natural killer cell activation |
| B | 0032872 | biological_process | regulation of stress-activated MAPK cascade |
| B | 0034101 | biological_process | erythrocyte homeostasis |
| B | 0042267 | biological_process | natural killer cell mediated cytotoxicity |
| B | 0042744 | biological_process | hydrogen peroxide catabolic process |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0045321 | biological_process | leukocyte activation |
| B | 0045454 | biological_process | cell redox homeostasis |
| B | 0051920 | molecular_function | peroxiredoxin activity |
| B | 0140824 | molecular_function | thioredoxin-dependent peroxiredoxin activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 301 |
| Chain | Residue |
| A | GLU55 |
| A | ARG128 |
| A | HOH252 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 302 |
| Chain | Residue |
| B | GLU55 |
| B | ARG128 |
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"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q06830","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q06830","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q06830","evidenceCode":"ECO:0000250"}]} |
| 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","evidences":[{"source":"UniProtKB","id":"Q06830","evidenceCode":"ECO:0000250"}]} |
| 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":"UniProtKB","id":"Q06830","evidenceCode":"ECO:0000250"}]} |
| 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 SUMO2)","evidences":[{"source":"UniProtKB","id":"Q06830","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
