Research workbench
Crystal structure of the C-terminal region of yeast CTF4, selenomethionine protein.
Analyse Crystal structure of the C-terminal region of yeast CTF4, selenomethionine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4C8H
- Type
- protein
- Length
- 1,275 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CTF4
- UniProt
- Q01454
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 3 distinct chains · 26% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CTF4 | protein | 431 | 28% helix, 33% strand | Q01454 |
| B | CTF4 | protein | 419 | 26% helix, 34% strand | Q01454 |
| C | CTF4 | protein | 425 | 26% helix, 34% strand | Q01454 |
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 667 | 0.81 | 0.86 | 71 | empty |
| 2 | 403 | 0.72 | 0.83 | 53 | empty |
| 3 | 631 | 0.69 | 0.77 | 71 | empty |
| 4 | 487 | 0.66 | 0.78 | 65 | empty |
| 5 | 265 | 0.64 | 0.81 | 45 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1490 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 1422 Ų buried · 16 hydrogen bonds · protein-protein
- A–C · 1398 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 31 modified (engineered).
Compared structures
- 4C8H · Crystal structure of the C-terminal region of yeast Ctf4, selenomethionine protein. · the same entry in another collection · chain A against A, TM-score 1.00
- Q01454 · AlphaFold monomer V2.0 prediction for DNA polymerase alpha-binding protein (Q01454) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q01454
- Elsewhere: RCSB PDB 4C8H · PDBe 4C8H · UniProt Q01454
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