MolNFT v1 · #23422 · protein
T. maritima nusb, P21
1TZT · N utilization substance protein B homolog: “T. maritima nusb, P21”. X-ray diffraction, 1 ligand (SO4), 3 pockets (best druggability 0.39). MolNFT v1 #23422 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1TZT
- Type
- protein
- Length
- 282 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N utilization substance protein B homolog
- UniProt
- Q9X286
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.39
Structure
x-ray diffraction · 1 distinct chain · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | N utilization substance protein B homolog | protein | 141 | 73% helix, 0% strand | Q9X286 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 52 | 0.39 | 0.81 | 11 | empty |
| 2 | 51 | 0.34 | 0.78 | 11 | empty |
| 3 | 74 | 0.28 | 0.72 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 166 Ų buried · 4 hydrogen bonds · protein-protein
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 Q9X286
- Elsewhere: RCSB PDB 1TZT · PDBe 1TZT · UniProt Q9X286
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