3A77
The crystal structure of phosphorylated IRF-3
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003700 | molecular_function | DNA-binding transcription factor activity |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0003700 | molecular_function | DNA-binding transcription factor activity |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| C | 0003700 | molecular_function | DNA-binding transcription factor activity |
| C | 0006355 | biological_process | regulation of DNA-templated transcription |
| D | 0003700 | molecular_function | DNA-binding transcription factor activity |
| D | 0006355 | biological_process | regulation of DNA-templated transcription |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACY A 2001 |
| Chain | Residue |
| A | GLN356 |
| A | PRO357 |
| A | TRP358 |
| A | HOH1019 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD A 3002 |
| Chain | Residue |
| A | PRO239 |
| A | ALA273 |
| A | TRP275 |
| A | HOH1856 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MPD B 3001 |
| Chain | Residue |
| B | PRO239 |
| B | TRP275 |
| B | GLN284 |
| B | HOH1101 |
| B | HOH1180 |
| B | GLU224 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACY C 2003 |
| Chain | Residue |
| C | GLN356 |
| C | PRO357 |
| C | TRP358 |
| C | HOH1215 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MPD C 3003 |
| Chain | Residue |
| C | GLU224 |
| C | PRO239 |
| C | TRP275 |
| C | GLN284 |
| C | HOH1203 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MPD D 3004 |
| Chain | Residue |
| D | GLU224 |
| D | PRO239 |
| D | TRP275 |
| D | HOH1075 |
| D | HOH1099 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 15 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23746807","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P70671","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22394562","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine; by TBK1","evidences":[{"source":"PubMed","id":"22394562","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23746807","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27302953","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36603579","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine; by IKKE and TBK1","evidences":[{"source":"PubMed","id":"22394562","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23478265","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27302953","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36603579","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23746807","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 16 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)","evidences":[{"source":"PubMed","id":"20308324","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
