Research workbench
Crystal structure of an ob-fold protein (TM0957) from thermotoga maritima MSB8 at 1.90 a resolution
Analyse Crystal structure of an ob-fold protein (TM0957) from thermotoga maritima MSB8… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2F4I
- Type
- protein
- Length
- 707 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein TM0957
- UniProt
- Q9X052
- Ligands
- MG, CL
- Pockets
- 8 · best druggability 0.77
Structure
x-ray diffraction · 3 distinct chains · 43% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Hypothetical protein TM0957 | protein | 176 | 43% helix, 28% strand | Q9X052 |
| B | Hypothetical protein TM0957 | protein | 178 | 43% helix, 28% strand | Q9X052 |
| C | Hypothetical protein TM0957 | protein | 177 | 43% helix, 28% strand | Q9X052 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1048 | 0.77 | 0.79 | 68 | empty |
| 2 | 358 | 0.59 | 0.76 | 48 | CL |
| 3 | 178 | 0.50 | 0.77 | 33 | empty |
| 4 | 149 | 0.49 | 0.78 | 24 | empty |
| 5 | 103 | 0.38 | 0.75 | 17 | empty |
Interfaces
4 interfaces between chains.
- C–D · 436 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 426 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 388 Ų buried · 1 hydrogen bond · protein-protein
- B–D · 248 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 69 modified (methylation, engineered).
Compared structures
- 2F4I · Crystal structure of an ob-fold protein (tm0957) from thermotoga maritima msb8 at 1.90 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 Q9X052
- Elsewhere: RCSB PDB 2F4I · PDBe 2F4I · UniProt Q9X052
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