Research workbench
Nucleosome assembly proteins I (nap-1, 74-365)
Analyse Nucleosome assembly proteins I (nap-1, 74-365) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Z2R
- Type
- protein
- Length
- 543 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nucleosome assembly protein
- UniProt
- P25293
- Pockets
- 7 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleosome assembly protein | protein | 275 | 44% helix, 17% strand | P25293 |
| B | Nucleosome assembly protein | protein | 268 | 45% helix, 20% strand | P25293 |
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 724 | 0.73 | 0.78 | 53 | empty |
| 2 | 128 | 0.44 | 0.77 | 14 | empty |
| 3 | 107 | 0.44 | 0.78 | 14 | empty |
| 4 | 55 | 0.40 | 0.82 | 13 | empty |
| 5 | 74 | 0.35 | 0.77 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 3449 Ų buried · 27 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 P25293
- Elsewhere: RCSB PDB 2Z2R · PDBe 2Z2R · UniProt P25293
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