Research workbench
Crystal structure of a phd finger bound to histone H3 K9ME3 peptide
Analyse Crystal structure of a phd finger bound to histone H3 K9ME3 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5FB1
- Type
- protein
- Length
- 182 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nuclear autoantigen sp-100; Peptide from histone H3
- UniProt
- P23497, K7EMV3
- Ligands
- ZN
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear autoantigen sp-100 | protein | 174 | 47% helix, 7% strand | P23497 |
| C | Peptide from histone H3 | protein | 8 | 0% helix, 50% strand | K7EMV3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–C · 613 Ų buried · 22 hydrogen bonds · protein-protein
Compared structures
- 5FB1 · Crystal Structure of a PHD finger bound to histone H3 K9me3 peptide · the same entry in another collection · chain A against A, TM-score 1.00
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 P23497
- Every structure of UniProt K7EMV3
- Elsewhere: RCSB PDB 5FB1 · PDBe 5FB1 · UniProt P23497 · UniProt K7EMV3
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