Research workbench
Human transcriptional coactivator PC4 C-terminal domain
Analyse Human transcriptional coactivator PC4 C-terminal domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PCF
- Type
- protein
- Length
- 528 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional coactivator PC4
- UniProt
- P53999
- Pockets
- 6 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | Transcriptional coactivator PC4 | protein | 66 | 30% helix, 52% strand | P53999 |
Pockets
6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 350 | 0.56 | 0.75 | 28 | empty |
| 2 | 318 | 0.55 | 0.75 | 25 | empty |
| 3 | 326 | 0.54 | 0.74 | 28 | empty |
| 4 | 184 | 0.52 | 0.78 | 22 | empty |
| 5 | 182 | 0.51 | 0.78 | 20 | empty |
Interfaces
14 interfaces between chains.
- C–D · 1495 Ų buried · 12 hydrogen bonds · protein-protein
- E–F · 1492 Ų buried · 13 hydrogen bonds · protein-protein
- G–H · 1490 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 1481 Ų buried · 13 hydrogen bonds · protein-protein
- E–H · 192 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 1PCF · Human transcriptional coactivator PC4 C-terminal domain · the same entry in another collection · chain C against C, TM-score 1.00
- P53999 · AlphaFold monomer V2.0 prediction for activated RNA polymerase II transcriptional… · a predicted model of the same protein · chain A against A, TM-score 0.95
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 P53999
- Elsewhere: RCSB PDB 1PCF · PDBe 1PCF · UniProt P53999
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