Research workbench
Crystal structure of caenorhabditis elegans NAP1
Analyse Crystal structure of caenorhabditis elegans NAP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6N2G
- Type
- protein
- Length
- 1,112 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nucleosome assembly protein
- UniProt
- Q19007
- Pockets
- 15 · best druggability 0.82
Structure
x-ray diffraction · 3 distinct chains · 43% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleosome assembly protein | protein | 285 | 43% helix, 18% strand | Q19007 |
| B, D | Nucleosome assembly protein | protein | 273 | 44% helix, 19% strand | Q19007 |
| C | Nucleosome assembly protein | protein | 281 | 43% helix, 17% strand | Q19007 |
Pockets
15 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1049 | 0.82 | 0.83 | 110 | empty |
| 2 | 950 | 0.72 | 0.76 | 73 | empty |
| 3 | 211 | 0.46 | 0.73 | 21 | empty |
| 4 | 221 | 0.46 | 0.73 | 28 | empty |
| 5 | 115 | 0.45 | 0.78 | 17 | empty |
Interfaces
5 interfaces between chains.
- B–C · 4377 Ų buried · 54 hydrogen bonds · protein-protein
- B–D · 588 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 327 Ų buried · 4 hydrogen bonds · protein-protein
- A–D · 250 Ų buried · 4 hydrogen bonds · protein-protein
- C–D · 26 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6N2G · Crystal structure of Caenorhabditis elegans NAP1 · 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 Q19007
- Elsewhere: RCSB PDB 6N2G · PDBe 6N2G · UniProt Q19007
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