Research workbench
Human MHF1-MHF2 complex
Analyse Human MHF1-MHF2 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4NE6
- Type
- protein
- Length
- 334 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Centromere protein S; Centromere protein X
- UniProt
- Q8N2Z9, A8MT69
- Pockets
- 2 · best druggability 0.61
Structure
x-ray diffraction · 2 distinct chains · 75% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Centromere protein S | protein | 93 | 80% helix, 4% strand | Q8N2Z9 |
| B, D | Centromere protein X | protein | 74 | 70% helix, 5% strand | A8MT69 |
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 | 364 | 0.61 | 0.77 | 49 | empty |
| 2 | 162 | 0.42 | 0.74 | 23 | empty |
Interfaces
6 interfaces between chains.
- C–D · 2398 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 2396 Ų buried · 15 hydrogen bonds · protein-protein
- A–C · 581 Ų buried · 11 hydrogen bonds · protein-protein
- B–D · 142 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 22 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 4NE6 · Human MHF1-MHF2 complex · the same entry in another collection · chain D against D, TM-score 1.00
- A8MT69 · AlphaFold monomer V2.0 prediction for centromere protein X (A8MT69) · a predicted model of the same protein · chain B against A, TM-score 0.99
- Q8N2Z9 · AlphaFold monomer V2.0 prediction for centromere protein S (Q8N2Z9) · 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 Q8N2Z9
- Every structure of UniProt A8MT69
- Elsewhere: RCSB PDB 4NE6 · PDBe 4NE6 · UniProt Q8N2Z9 · UniProt A8MT69
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