Research workbench
Crystal structure of NURF55 in complex with a H4 peptide
Analyse Crystal structure of NURF55 in complex with a H4 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XYI
- Type
- protein
- Length
- 393 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable histone-binding protein CAF1; Histone H4
- UniProt
- Q24572, P84040
- Pockets
- 3 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 13% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable histone-binding protein CAF1 | protein | 379 | 11% helix, 44% strand | Q24572 |
| B | Histone H4 | protein | 14 | 64% helix, 0% strand | P84040 |
Ligands and binding sites
- PG4 · Tetraethylene glycol · additive · 3 copies · chains A
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 437 | 0.76 | 0.85 | 33 | empty |
| 2 | 87 | 0.47 | 0.81 | 14 | PG4 |
| 3 | 82 | 0.45 | 0.81 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 786 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 2XYI · Crystal Structure of Nurf55 in complex with a H4 peptide · the same entry in another collection · chain A against A, TM-score 1.00
- Q24572 · AlphaFold monomer V2.0 prediction for chromatin assembly factor 1 P55 subunit (Q24572) · a predicted model of the same protein · chain A against A, TM-score 0.99
- P84040 · AlphaFold monomer V2.0 prediction for histone H4 (P84040) · a predicted model of the same protein · chain B against A, TM-score 0.77
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 Q24572
- Every structure of UniProt P84040
- Elsewhere: RCSB PDB 2XYI · PDBe 2XYI · UniProt Q24572 · UniProt P84040
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