MolNFT v1 · #18907 · protein
Chromodomain of HP1 complexed with histone H3 tail containing monomethyllysine 9.
1Q3L · Heterochromatin protein 1: “Chromodomain of HP1 complexed with histone H3 tail containing monomethyllysine 9.”. X-ray diffraction. MolNFT v1 #18907 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1Q3L
- Type
- protein
- Length
- 58 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heterochromatin protein 1; Histone H3
- UniProt
- P05205, P16106
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heterochromatin protein 1 | protein | 52 | 31% helix, 50% strand | P05205 |
| P | Histone H3 | protein | 6 | 0% helix, 33% strand | P16106 |
Interfaces
1 interface between chains.
- A–P · 544 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (methylation).
Compared structures
- 1Q3L · Chromodomain Of HP1 Complexed With Histone H3 Tail Containing monomethyllysine 9. · the same entry in another collection · chain A against A, TM-score 1.00
- P05205 · AlphaFold monomer V2.0 prediction for heterochromatin protein 1 (P05205) · 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 P05205
- Every structure of UniProt P16106
- Elsewhere: RCSB PDB 1Q3L · PDBe 1Q3L · UniProt P05205 · UniProt P16106
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