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
- 4NE3
- Type
- protein
- Length
- 167 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Centromere protein S; Centromere protein X
- UniProt
- Q8N2Z9, A8MT69
Structure
x-ray diffraction · 2 distinct chains · 74% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Centromere protein S | protein | 93 | 78% helix, 3% strand | Q8N2Z9 |
| B | Centromere protein X | protein | 74 | 69% helix, 4% strand | A8MT69 |
Interfaces
1 interface between chains.
- A–B · 2355 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified (engineered).
Compared structures
- 4NE3 · Human MHF1-MHF2 complex · the same entry in another collection · chain A against A, 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 4NE3 · PDBe 4NE3 · UniProt Q8N2Z9 · UniProt A8MT69
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