4OY2
Crystal structure of TAF1-TAF7, a TFIID subcomplex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004402 | molecular_function | histone acetyltransferase activity |
| A | 0005669 | cellular_component | transcription factor TFIID complex |
| A | 0006366 | biological_process | transcription by RNA polymerase II |
| A | 0016251 | molecular_function | RNA polymerase II general transcription initiation factor activity |
| A | 0017025 | molecular_function | TBP-class protein binding |
| B | 0005669 | cellular_component | transcription factor TFIID complex |
| B | 0006367 | biological_process | transcription initiation at RNA polymerase II promoter |
| C | 0004402 | molecular_function | histone acetyltransferase activity |
| C | 0005669 | cellular_component | transcription factor TFIID complex |
| C | 0006366 | biological_process | transcription by RNA polymerase II |
| C | 0016251 | molecular_function | RNA polymerase II general transcription initiation factor activity |
| C | 0017025 | molecular_function | TBP-class protein binding |
| D | 0005669 | cellular_component | transcription factor TFIID complex |
| D | 0006367 | biological_process | transcription initiation at RNA polymerase II promoter |
| E | 0004402 | molecular_function | histone acetyltransferase activity |
| E | 0005669 | cellular_component | transcription factor TFIID complex |
| E | 0006366 | biological_process | transcription by RNA polymerase II |
| E | 0016251 | molecular_function | RNA polymerase II general transcription initiation factor activity |
| E | 0017025 | molecular_function | TBP-class protein binding |
| F | 0005669 | cellular_component | transcription factor TFIID complex |
| F | 0006367 | biological_process | transcription initiation at RNA polymerase II promoter |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | binding site for residue ZN A 1001 |
| Chain | Residue |
| B | ASP109 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue TRS D 401 |
| Chain | Residue |
| D | ARG179 |
| D | LYS180 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 60 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 51 |
| Details | Compositional bias: {"description":"Low complexity","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
