Research workbench
The heterotrimeric complex of kluyveromyces lactis SCM3, CSE4 and H4
Analyse The heterotrimeric complex of kluyveromyces lactis SCM3, CSE4 and H4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2YFV
- Type
- protein
- Length
- 202 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone H3-like centromeric protein CSE4; Histone H4; SCM3
- UniProt
- Q6CTI2, Q6CMU6, Q6CL77
- Ligands
- IOD
- Pockets
- 2 · best druggability 0.48
Structure
x-ray diffraction · 3 distinct chains · 65% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone H3-like centromeric protein CSE4 | protein | 68 | 74% helix, 6% strand | Q6CTI2 |
| B | Histone H4 | protein | 74 | 69% helix, 5% strand | Q6CMU6 |
| C | SCM3 | protein | 60 | 50% helix, 13% strand | Q6CL77 |
Ligands and binding sites
- IOD · Iodide ion · ion · 2 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 117 | 0.48 | 0.79 | 18 | IOD |
| 2 | 83 | 0.36 | 0.76 | 14 | empty |
Interfaces
3 interfaces between chains.
- A–B · 2000 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 976 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 472 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 2YFV · The heterotrimeric complex of Kluyveromyces lactis Scm3, Cse4 and H4 · the same entry in another collection · chain A against A, TM-score 1.00
- Q6CTI2 · AlphaFold monomer V2.0 prediction for histone H3-like centromeric protein CSE4 (Q6CTI2) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 Q6CTI2
- Every structure of UniProt Q6CMU6
- Every structure of UniProt Q6CL77
- Elsewhere: RCSB PDB 2YFV · PDBe 2YFV · UniProt Q6CTI2 · UniProt Q6CMU6 · UniProt Q6CL77
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