MolNFT v1 · #148340 · protein
Crystal structure of the human TAF5-TAF6-TAF9 complex
6F3T · Transcription initiation factor tfiid subunit 5: “Crystal structure of the human TAF5-TAF6-TAF9 complex”. X-ray diffraction, 1 ligand (CL), 20 pockets (best druggability 0.86). MolNFT v1 #148340 on GenesisL1: 3D structure, binding…
- PDB
- 6F3T
- Type
- protein
- Length
- 3,040 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcription initiation factor tfiid subunit 5; Transcription initiation factor tfiid…
- UniProt
- Q15542, P49848, Q16594
- Ligands
- CL
- Pockets
- 20 · best druggability 0.86
Structure
x-ray diffraction · 8 distinct chains · 32% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcription initiation factor tfiid subunit 5 | protein | 552 | 28% helix, 31% strand | Q15542 |
| B | Transcription initiation factor tfiid subunit 5 | protein | 551 | 27% helix, 31% strand | Q15542 |
| C | Transcription initiation factor tfiid subunit 5 | protein | 551 | 28% helix, 31% strand | Q15542 |
| D | Transcription initiation factor tfiid subunit 5 | protein | 550 | 28% helix, 31% strand | Q15542 |
| E, K | Transcription initiation factor tfiid subunit 6 | protein | 93 | 52% helix, 8% strand | P49848 |
| F, H, J, L | Transcription initiation factor tfiid subunit 9 | protein | 116 | 54% helix, 1% strand | Q16594 |
| G | Transcription initiation factor tfiid subunit 6 | protein | 92 | 52% helix, 8% strand | P49848 |
| I | Transcription initiation factor tfiid subunit 6 | protein | 94 | 51% helix, 9% strand | P49848 |
Ligands and binding sites
- CL · Chloride ion · ion · 7 copies · chains A, E, B, C, G, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 845 | 0.86 | 0.89 | 94 | CL |
| 2 | 879 | 0.86 | 0.88 | 80 | CL |
| 3 | 812 | 0.85 | 0.88 | 80 | CL |
| 4 | 803 | 0.85 | 0.88 | 87 | CL |
| 5 | 931 | 0.85 | 0.86 | 95 | empty |
Interfaces
40 interfaces between chains.
- E–F · 2325 Ų buried · 20 hydrogen bonds · protein-protein
- I–J · 2299 Ų buried · 19 hydrogen bonds · protein-protein
- K–L · 2271 Ų buried · 19 hydrogen bonds · protein-protein
- G–H · 2201 Ų buried · 21 hydrogen bonds · protein-protein
- D–L · 1498 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (phosphorylation).
Compared structures
- 6F3T · Crystal structure of the human TAF5-TAF6-TAF9 complex · the same entry in another collection · chain L against L, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q15542
- Every structure of UniProt P49848
- Every structure of UniProt Q16594
- Elsewhere: RCSB PDB 6F3T · PDBe 6F3T · UniProt Q15542 · UniProt P49848 · UniProt Q16594
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