Research workbench
General transcription factor tfiih (weak binding)
Analyse General transcription factor tfiih (weak binding) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7ML3
- Type
- protein + DNA
- Length
- 3,028 residues
- Chains
- 10
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- BJ4_G0050160.MRNA.1.CDS.1; RNA polymerase II transcription factor B subunit 2; General…
- EC
- 3.6.4.12
- UniProt
- A0A7I9BTI9, A0A6A5Q2X3, A0A6A5Q1C1, A0A7I9C5C2, A0A7I9FQL5, Q3E7C1, Q00578
- Ligands
- SF4, ZN
- Pockets
- 20 · best druggability 0.85
Structure
electron microscopy · 10 distinct chains · 45% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| 3 | BJ4_G0050160.MRNA.1.CDS.1 | protein | 138 | 43% helix, 1% strand | A0A7I9BTI9 |
| 2 | RNA polymerase II transcription factor B subunit 2 | protein | 460 | 49% helix, 5% strand | A0A6A5Q2X3 |
| 0 | General transcription and DNA repair factor iih helicase subunit xpd (EC 3.6.4.12) | protein | 754 | 51% helix, 10% strand | A0A6A5Q1C1 |
| 1 | TFB1 | protein | 367 | 67% helix, 0% strand | — |
| 4 | General transcription and DNA repair factor iih subunit TFB4 | protein | 284 | 35% helix, 13% strand | A0A7I9C5C2 |
| 6 | General transcription and DNA repair factor iih | protein | 351 | 28% helix, 13% strand | A0A7I9FQL5 |
| 5 | General transcription and DNA repair factor iih subunit TFB5 | protein | 66 | 44% helix, 21% strand | Q3E7C1 |
| 7 | General transcription and DNA repair factor iih helicase subunit xpb (EC 3.6.4.12) | protein | 548 | 37% helix, 11% strand | Q00578 |
| N | Non-template strand DNA | dna | 30 | — | — |
| T | Template strand DNA | dna | 30 | — | — |
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 | 939 | 0.85 | 0.86 | 108 | empty |
| 2 | 757 | 0.82 | 0.85 | 97 | empty |
| 3 | 725 | 0.81 | 0.84 | 77 | empty |
| 4 | 527 | 0.80 | 0.86 | 97 | empty |
| 5 | 520 | 0.77 | 0.84 | 57 | empty |
Interfaces
17 interfaces between chains.
- 0–1 · 2330 Ų buried · 33 hydrogen bonds · protein-protein
- 4–6 · 1730 Ų buried · 16 hydrogen bonds · protein-protein
- N–T · 1391 Ų buried · 110 hydrogen bonds · nucleic-nucleic
- 1–6 · 1129 Ų buried · 11 hydrogen bonds · protein-protein
- 2–5 · 927 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 7ML3 · General transcription factor TFIIH (weak binding) · the same entry in another collection · chain N against N, TM-score 1.00
- Q00578 · 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 0.87
- Q3E7C1 · AlphaFold monomer V2.0 prediction for general transcription and DNA repair factor iih… · a predicted model of the same protein · chain 5 against A, TM-score 0.76
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 A0A7I9BTI9
- Every structure of UniProt A0A6A5Q2X3
- Every structure of UniProt A0A6A5Q1C1
- Every structure of UniProt A0A7I9C5C2
- Every structure of UniProt A0A7I9FQL5
- Every structure of UniProt Q3E7C1
- Every structure of UniProt Q00578
- Elsewhere: RCSB PDB 7ML3 · PDBe 7ML3 · UniProt A0A7I9BTI9 · UniProt A0A6A5Q2X3 · UniProt A0A6A5Q1C1 · UniProt A0A7I9C5C2 · UniProt A0A7I9FQL5 · UniProt Q3E7C1 · UniProt Q00578
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.