Research workbench
NMR structure of the complex between the TFB1 subunit of tfiih and the activation domain of eklf
Analyse NMR structure of the complex between the TFB1 subunit of tfiih and the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2L2I
- Type
- protein
- Length
- 142 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA polymerase II transcription factor B subunit 1; Krueppel-like factor 1
- UniProt
- P32776, Q13351
- Pockets
- 1 · best druggability 0.26
Structure
solution nmr · 2 distinct chains · 15% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RNA polymerase II transcription factor B subunit 1 | protein | 115 | 19% helix, 32% strand | P32776 |
| B | Krueppel-like factor 1 | protein | 27 | 0% helix, 0% strand | Q13351 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 54 | 0.26 | 0.73 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 757 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 2L2I · NMR Structure of the complex between the Tfb1 subunit of TFIIH and the activation domain… · the same entry in another collection · chain A against A, TM-score 1.00
- P32776 · AlphaFold monomer V2.0 prediction for general transcription and DNA repair factor iih… · a predicted model of the same protein · chain A against A, TM-score 0.79
- Q13351 · AlphaFold monomer V2.0 prediction for krueppel-like factor 1 (Q13351) · a predicted model of the same protein · chain B against A, TM-score 0.28
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 P32776
- Every structure of UniProt Q13351
- Elsewhere: RCSB PDB 2L2I · PDBe 2L2I · UniProt P32776 · UniProt Q13351
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