Research workbench
CDC27 N-terminus
Analyse CDC27 N-terminus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3KAE
- Type
- protein
- Length
- 914 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Possible protein of nuclear scaffold
- UniProt
- Q8SQV4
- Ligands
- CL, SO4
- Pockets
- 11 · best druggability 0.72
Structure
x-ray diffraction · 3 distinct chains · 70% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Possible protein of nuclear scaffold | protein | 225 | 70% helix, 1% strand | Q8SQV4 |
| B, C | Possible protein of nuclear scaffold | protein | 231 | 69% helix, 1% strand | Q8SQV4 |
| D | Possible protein of nuclear scaffold | protein | 227 | 70% helix, 1% strand | Q8SQV4 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A, C
- SO4 · Sulfate ion · ion · chains D
- GOL · Glycerol · additive · 3 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 293 | 0.72 | 0.86 | 20 | CL |
| 2 | 310 | 0.72 | 0.84 | 21 | empty |
| 3 | 456 | 0.67 | 0.79 | 53 | empty |
| 4 | 436 | 0.67 | 0.79 | 50 | empty |
| 5 | 58 | 0.56 | 0.89 | 17 | empty |
Interfaces
3 interfaces between chains.
- B–D · 2210 Ų buried · 19 hydrogen bonds · protein-protein
- A–C · 2081 Ų buried · 16 hydrogen bonds · protein-protein
- C–D · 85 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3KAE · Cdc27 N-terminus · the same entry in another collection · chain A against A, TM-score 1.00
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 Q8SQV4
- Elsewhere: RCSB PDB 3KAE · PDBe 3KAE · UniProt Q8SQV4
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