Research workbench
NMR structure of the complex between the pH domain of the TFB1 subunit from tfiih and the N-terminal activation domain of eklf (TAD1)
Analyse NMR structure of the complex between the pH domain of the TFB1 subunit from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2N23
- Type
- protein
- Length
- 134 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 0.40
Structure
solution nmr · 2 distinct chains · 29% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RNA polymerase II transcription factor B subunit 1 | protein | 115 | 20% helix, 39% strand | P32776 |
| B | Krueppel-like factor 1 | protein | 19 | 84% 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 | 119 | 0.40 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 421 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 2N23 · NMR structure of the complex between the PH domain of the Tfb1 subunit from TFIIH and the… · 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 0.81
- 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 0.50
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 2N23 · PDBe 2N23 · UniProt P32776 · UniProt Q13351
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