Research workbench
Crystal structure of an osmc-like protein (GSU2788) from geobacter sulfurreducens at 1.50 a resolution
Analyse Crystal structure of an osmc-like protein (GSU2788) from geobacter… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OPL
- Type
- protein
- Length
- 363 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein
- UniProt
- Q749F5
- Ligands
- NA, SO4
- Pockets
- 2 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical protein | protein | 181 | 35% helix, 31% strand | Q749F5 |
| B | Hypothetical protein | protein | 182 | 35% helix, 32% strand | Q749F5 |
Ligands and binding sites
- NA · Sodium ion · metal · chains A, B
- SO4 · Sulfate ion · ion · chains B
- ACT · Acetate ion · additive · chains A, B
- P6G · Hexaethylene glycol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 138 | 0.79 | 0.96 | 28 | empty |
| 2 | 116 | 0.79 | 0.97 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 5424 Ų buried · 79 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 9 modified (engineered, oxidation).
Compared structures
- 2OPL · Crystal structure of an osmc-like protein (gsu2788) from geobacter sulfurreducens at 1.50… · 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 Q749F5
- Elsewhere: RCSB PDB 2OPL · PDBe 2OPL · UniProt Q749F5
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