1OC3
HUMAN PEROXIREDOXIN 5
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008379 | molecular_function | thioredoxin peroxidase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0034599 | biological_process | cellular response to oxidative stress |
| B | 0008379 | molecular_function | thioredoxin peroxidase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0034599 | biological_process | cellular response to oxidative stress |
| C | 0008379 | molecular_function | thioredoxin peroxidase activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0034599 | biological_process | cellular response to oxidative stress |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BEZ A 201 |
| Chain | Residue |
| A | PRO40 |
| A | THR44 |
| A | GLY46 |
| A | CYS47 |
| A | ARG127 |
| C | ALA64 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BEZ B 201 |
| Chain | Residue |
| B | PRO40 |
| B | THR44 |
| B | GLY46 |
| B | CYS47 |
| B | ARG127 |
| A | LYS63 |
| A | ALA64 |
| A | GLY66 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 474 |
| Details | Domain: {"description":"Thioredoxin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00691","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Motif: {"description":"Microbody targeting signal","evidences":[{"source":"PubMed","id":"10514471","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Cysteine sulfenic acid (-SOH) intermediate","evidences":[{"source":"PubMed","id":"10751410","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"20643143","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P99029","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P99029","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P99029","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9R063","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P99029","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 3 |
| Details | Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"31740833","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
