Research workbench
NMR structure of the complex between the pH domain of the TFB1 subunit from tfiih and the activation domain of P53
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
- 2GS0
- Type
- protein
- Length
- 129 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA polymerase II transcription factor B subunit 1; Cellular tumor antigen P53
- UniProt
- P32776, P04637
Structure
solution nmr · 2 distinct chains · 28% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RNA polymerase II transcription factor B subunit 1 | protein | 115 | 23% helix, 40% strand | P32776 |
| B | Cellular tumor antigen P53 | protein | 14 | 64% helix, 0% strand | P04637 |
Interfaces
1 interface between chains.
- A–B · 408 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 2GS0 · 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 0.87
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 P04637
- Elsewhere: RCSB PDB 2GS0 · PDBe 2GS0 · UniProt P32776 · UniProt P04637
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