Research workbench
Crystal structure of a putative nucleotide binding protein (TM0796) from thermotoga maritima at 2.67 a resolution
Analyse Crystal structure of a putative nucleotide binding protein (TM0796) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2G0T
- Type
- protein
- Length
- 676 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Conserved hypothetical protein
- Ligands
- PO4
- Pockets
- 6 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Conserved hypothetical protein | protein | 337 | 38% helix, 18% strand | — |
| B | Conserved hypothetical protein | protein | 339 | 39% helix, 17% strand | — |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 3 copies · chains A, B
- FMT · Formic acid · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 785 | 0.76 | 0.80 | 70 | PO4 |
| 2 | 546 | 0.70 | 0.79 | 47 | PO4, EDO |
| 3 | 118 | 0.50 | 0.80 | 26 | empty |
| 4 | 52 | 0.45 | 0.84 | 19 | empty |
| 5 | 61 | 0.38 | 0.79 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1562 Ų buried · 19 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 2G0T · Crystal structure of a putative nucleotide binding protein (tm0796) from Thermotoga… · 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
- Elsewhere: RCSB PDB 2G0T · PDBe 2G0T
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