Research workbench
Structural insights into nucleosome reorganization by NAP1-related protein 1 (NRP1)
Analyse Structural insights into nucleosome reorganization by NAP1-related protein 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7BP5
- Type
- protein
- Length
- 177 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9LD28, Q9LQQ4
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 82 | — | Q9LD28 |
| B | — | protein | 90 | — | Q9LQQ4 |
| C | — | protein | 5 | — | — |
Ligands and binding sites
- GOL · Glycerol · additive · chains B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7BP5 · Structural insights into nucleosome reorganization by NAP1-RELATED PROTEIN 1 (NRP1) · the same entry in another collection · chain A against A, TM-score 1.00
- Q9LD28 · AlphaFold monomer V2.0 prediction for histone H2A.6 (Q9LD28) · a predicted model of the same protein · chain A against A, TM-score 0.96
- Q9LQQ4 · AlphaFold monomer V2.0 prediction for histone H2B.1 (Q9LQQ4) · a predicted model of the same protein · chain B against A, TM-score 0.94
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 Q9LD28
- Every structure of UniProt Q9LQQ4
- Elsewhere: RCSB PDB 7BP5 · PDBe 7BP5 · UniProt Q9LD28 · UniProt Q9LQQ4
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