Research workbench
Heterotrimeric interaction between RFX5 and rfxap
Analyse Heterotrimeric interaction between RFX5 and rfxap in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2KW3
- Type
- protein
- Length
- 198 residues
- Chains
- 3
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA-binding protein RFX5; Regulatory factor X-associated protein
- UniProt
- P48382, O00287
- Pockets
- 2 · best druggability 0.64
Structure
solution nmr · 2 distinct chains · 50% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | DNA-binding protein RFX5 | protein | 68 | 53% helix, 0% strand | P48382 |
| C | Regulatory factor X-associated protein | protein | 62 | 47% helix, 0% strand | O00287 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 58 | 0.64 | 0.93 | 19 | empty |
| 2 | 90 | 0.35 | 0.74 | 17 | empty |
Interfaces
3 interfaces between chains.
- A–C · 967 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 863 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 629 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 2KW3 · Heterotrimeric interaction between RFX5 and RFXAP · the same entry in another collection · chain A against A, TM-score 1.00
- O00287 · AlphaFold monomer V2.0 prediction for regulatory factor X-associated protein (O00287) · a predicted model of the same protein · chain C against A, TM-score 0.36
- P48382 · AlphaFold monomer V2.0 prediction for DNA-binding protein RFX5 (P48382) · a predicted model of the same protein · chain A against A, TM-score 0.35
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 P48382
- Every structure of UniProt O00287
- Elsewhere: RCSB PDB 2KW3 · PDBe 2KW3 · UniProt P48382 · UniProt O00287
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