Research workbench
CBX3 chromo shadow domain in complex with histone H3 peptide
Analyse CBX3 chromo shadow domain in complex with histone H3 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5T1I
- Type
- protein
- Length
- 151 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chromobox protein homolog 3; Histone H3.1
- UniProt
- Q13185, P68431
- Ligands
- UNX
Structure
x-ray diffraction · 2 distinct chains · 24% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Chromobox protein homolog 3 | protein | 68 | 29% helix, 31% strand | Q13185 |
| C | Histone H3.1 | protein | 15 | 0% helix, 47% strand | P68431 |
Ligands and binding sites
- UNX · Unknown atom or ion · ion · 12 copies · chains A, C, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- A–B · 678 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 622 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 569 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
Compared structures
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 Q13185
- Every structure of UniProt P68431
- Elsewhere: RCSB PDB 5T1I · PDBe 5T1I · UniProt Q13185 · UniProt P68431
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