MolNFT v1 · #25258 · protein
Crystal structure of a DUF1893 family protein (TM1506) from thermotoga maritima at 2.70 a resolution
1VK9 · Conserved hypothetical protein TM1506: “Crystal structure of a DUF1893 family protein (TM1506) from thermotoga maritima at 2.70 a resolution”. X-ray diffraction, 2 ligands (UNL, ZN), 2 pockets (best druggability 0.52). MolNFT v1…
- PDB
- 1VK9
- Type
- protein
- Length
- 147 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Conserved hypothetical protein TM1506
- UniProt
- Q9X1J4
- Ligands
- UNL, ZN
- Pockets
- 2 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Conserved hypothetical protein TM1506 | protein | 147 | 39% helix, 22% strand | Q9X1J4 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 131 | 0.52 | 0.81 | 26 | UNL |
| 2 | 73 | 0.38 | 0.78 | 14 | empty |
Modifications
Observed in the structure: 5 modified, 1 covalent (engineered, covalent ligand).
Compared structures
- 1VK9 · CRYSTAL STRUCTURE OF A DUF1893 family protein (TM1506) FROM THERMOTOGA MARITIMA AT 2.70 A… · 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 Q9X1J4
- Elsewhere: RCSB PDB 1VK9 · PDBe 1VK9 · UniProt Q9X1J4
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