4DSS
Crystal structure of peroxiredoxin Ahp1 from Saccharomyces cerevisiae in complex with thioredoxin Trx2
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005777 | cellular_component | peroxisome |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008379 | molecular_function | thioredoxin peroxidase activity |
| A | 0010038 | biological_process | response to metal ion |
| A | 0016209 | molecular_function | antioxidant activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0034599 | biological_process | cellular response to oxidative stress |
| A | 0042744 | biological_process | hydrogen peroxide catabolic process |
| A | 0045454 | biological_process | cell redox homeostasis |
| A | 0050821 | biological_process | protein stabilization |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| A | 0140824 | molecular_function | thioredoxin-dependent peroxiredoxin activity |
| B | 0000011 | biological_process | vacuole inheritance |
| B | 0000103 | biological_process | sulfate assimilation |
| B | 0000139 | cellular_component | Golgi membrane |
| B | 0000324 | cellular_component | fungal-type vacuole |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006749 | biological_process | glutathione metabolic process |
| B | 0006888 | biological_process | endoplasmic reticulum to Golgi vesicle-mediated transport |
| B | 0006890 | biological_process | retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum |
| B | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| B | 0015031 | biological_process | protein transport |
| B | 0015035 | molecular_function | protein-disulfide reductase activity |
| B | 0015036 | molecular_function | disulfide oxidoreductase activity |
| B | 0042144 | biological_process | vacuole fusion, non-autophagic |
| B | 0045454 | biological_process | cell redox homeostasis |
| B | 0120124 | cellular_component | membrane fusion priming complex |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 269 |
| Details | Domain: {"description":"Thioredoxin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00691","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Cysteine sulfenic acid (-SOH) intermediate","evidences":[{"source":"PubMed","id":"22474296","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Cysteine persulfide","evidences":[{"source":"PubMed","id":"36102610","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in URM1)","evidences":[{"source":"PubMed","id":"32004955","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36102610","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21209336","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in URM1); alternate","evidences":[{"source":"PubMed","id":"32004955","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36102610","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in URM1); alternate","evidences":[{"source":"PubMed","id":"36102610","evidenceCode":"ECO:0000269"}]} |
| 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 URM1)","evidences":[{"source":"PubMed","id":"36102610","evidenceCode":"ECO:0000269"}]} |
| 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 ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | Site: {"description":"Deprotonates C-terminal active site Cys"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | Site: {"description":"Contributes to redox potential value"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
