MolNFT v1 · #39660 · protein
Crystal structure analysis of NP24-I, a thaumatin-like protein
2I0W · Protein NP24: “Crystal structure analysis of NP24-I, a thaumatin-like protein”. X-ray diffraction, 1 ligand (CL), 1 pocket (best druggability 0.33). MolNFT v1 #39660 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2I0W
- Type
- protein
- Length
- 207 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein NP24
- UniProt
- P12670
- Ligands
- CL
- Pockets
- 1 · best druggability 0.33
Structure
x-ray diffraction · 1 distinct chain · 9% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein NP24 | protein | 207 | 9% helix, 37% strand | P12670 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 85 | 0.33 | 0.74 | 19 | empty |
Modifications
Observed in the structure: 8 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 P12670
- Elsewhere: RCSB PDB 2I0W · PDBe 2I0W · UniProt P12670
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