MolNFT v1 · #56332 · protein
Crystal structure of uncharacterized conserved protein from thermotoga maritima
2ZBU: “Crystal structure of uncharacterized conserved protein from thermotoga maritima”. X-ray diffraction, 1 ligand (ADN), 14 pockets (best druggability 0.78). MolNFT v1 #56332 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2ZBU
- Type
- protein
- Length
- 1,052 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized conserved protein
- UniProt
- Q9WZC8
- Ligands
- ADN
- Pockets
- 14 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Uncharacterized conserved protein | protein | 263 | 24% helix, 30% strand | Q9WZC8 |
Ligands and binding sites
- ADN · Adenosine · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1186 | 0.78 | 0.80 | 119 | empty |
| 2 | 811 | 0.71 | 0.76 | 77 | empty |
| 3 | 155 | 0.56 | 0.81 | 24 | empty |
| 4 | 167 | 0.54 | 0.80 | 27 | empty |
| 5 | 145 | 0.41 | 0.74 | 19 | empty |
Interfaces
5 interfaces between chains.
- A–C · 335 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 332 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 283 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 14 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 13 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 modified (engineered).
Compared structures
- 2ZBU · Crystal structure of uncharacterized conserved protein from Thermotoga maritima · 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 Q9WZC8
- Elsewhere: RCSB PDB 2ZBU · PDBe 2ZBU · UniProt Q9WZC8
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