MolNFT v1 · #158948 · protein
Structure of the human apo tfiih
6O9M · Tfiih basal transcription factor complex helicase xpd…: “Structure of the human apo tfiih”. Electron microscopy, 2 ligands (SF4, ZN), 20 pockets (best druggability 0.88). MolNFT v1 #158948 on GenesisL1: 3D structure, binding sites…
- PDB
- 6O9M
- Type
- protein
- Length
- 3,228 residues
- Chains
- 8
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tfiih basal transcription factor complex helicase xpd subunit; General transcription…
- EC
- 3.6.4.12
- UniProt
- P18074, P32780, Q92759, P51948, Q13889, Q6ZYL4, Q13888, P19447
- Ligands
- SF4, ZN
- Pockets
- 20 · best druggability 0.88
Structure
electron microscopy · 8 distinct chains · 40% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| 0 | Tfiih basal transcription factor complex helicase xpd subunit (EC 3.6.4.12) | protein | 732 | 43% helix, 7% strand | P18074 |
| 1 | General transcription factor iih subunit 1 | protein | 433 | 57% helix, 0% strand | P32780 |
| 2 | General transcription factor iih subunit 4, P52 | protein | 453 | 39% helix, 4% strand | Q92759 |
| 3 | Cdk-activating kinase assembly factor MAT1 | protein | 212 | 53% helix, 3% strand | P51948 |
| 4 | General transcription factor iih subunit 3 | protein | 295 | 29% helix, 9% strand | Q13889 |
| 5 | General transcription factor iih subunit 5 | protein | 66 | 41% helix, 12% strand | Q6ZYL4 |
| 6 | General transcription factor iih subunit 2 | protein | 385 | 31% helix, 14% strand | Q13888 |
| 7 | Tfiih basal transcription factor complex helicase xpb subunit (EC 3.6.4.12) | protein | 652 | 35% helix, 9% strand | P19447 |
Ligands and binding sites
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 | 582 | 0.88 | 0.93 | 104 | empty |
| 2 | 587 | 0.87 | 0.93 | 102 | empty |
| 3 | 654 | 0.86 | 0.90 | 105 | empty |
| 4 | 308 | 0.84 | 0.94 | 63 | empty |
| 5 | 252 | 0.82 | 0.95 | 50 | empty |
Interfaces
14 interfaces between chains.
- 0–1 · 3248 Ų buried · 34 hydrogen bonds · protein-protein
- 1–4 · 2758 Ų buried · 28 hydrogen bonds · protein-protein
- 4–6 · 2410 Ų buried · 15 hydrogen bonds · protein-protein
- 1–6 · 2343 Ų buried · 23 hydrogen bonds · protein-protein
- 2–4 · 1890 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 6O9M · Structure of the human apo TFIIH · the same entry in another collection · chain 7 against 7, TM-score 1.00
- P18074 · AlphaFold monomer V2.0 prediction for general transcription and DNA repair factor iih… · a predicted model of the same protein · chain 0 against A, TM-score 0.95
- P19447 · AlphaFold monomer V2.0 prediction for general transcription and DNA repair factor iih… · a predicted model of the same protein · chain 7 against A, TM-score 0.90
- Q13888 · AlphaFold monomer V2.0 prediction for general transcription factor iih subunit 2 (Q13888) · a predicted model of the same protein · chain 6 against A, TM-score 0.87
- Q13889 · AlphaFold monomer V2.0 prediction for general transcription factor iih subunit 3 (Q13889) · a predicted model of the same protein · chain 4 against A, TM-score 0.85
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 P18074
- Every structure of UniProt P32780
- Every structure of UniProt Q92759
- Every structure of UniProt P51948
- Every structure of UniProt Q13889
- Every structure of UniProt Q6ZYL4
- Every structure of UniProt Q13888
- Every structure of UniProt P19447
- Elsewhere: RCSB PDB 6O9M · PDBe 6O9M · UniProt P18074 · UniProt P32780 · UniProt Q92759 · UniProt P51948 · UniProt Q13889 · UniProt Q6ZYL4 · UniProt Q13888 · UniProt P19447
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