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Crystal structure of a phou-like protein (SO_3770) from shewanella oneidensis mr-1 at 2.00 a resolution
Analyse Crystal structure of a phou-like protein (SO_3770) from shewanella oneidensis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OLT
- Type
- protein
- Length
- 642 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein
- UniProt
- Q8EAX1
- Ligands
- CL
- Pockets
- 8 · best druggability 0.59
Structure
x-ray diffraction · 3 distinct chains · 86% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical protein | protein | 214 | 87% helix, 0% strand | Q8EAX1 |
| B | Hypothetical protein | protein | 211 | 89% helix, 0% strand | Q8EAX1 |
| C | Hypothetical protein | protein | 217 | 84% helix, 0% strand | Q8EAX1 |
Ligands and binding sites
- CL · Chloride ion · ion · 3 copies · chains A, B, C
- GOL · Glycerol · additive · 4 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 570 | 0.59 | 0.73 | 52 | empty |
| 2 | 195 | 0.58 | 0.80 | 31 | empty |
| 3 | 110 | 0.54 | 0.83 | 25 | empty |
| 4 | 284 | 0.52 | 0.74 | 35 | empty |
| 5 | 118 | 0.50 | 0.80 | 19 | empty |
Interfaces
2 interfaces between chains.
- B–C · 447 Ų buried · 1 hydrogen bond · protein-protein
- A–C · 285 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 15 modified (engineered).
Compared structures
- 2OLT · Crystal structure of a phou-like protein (so_3770) from shewanella oneidensis mr-1 at… · 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 Q8EAX1
- Elsewhere: RCSB PDB 2OLT · PDBe 2OLT · UniProt Q8EAX1
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