Research workbench
Crystal structure of prox from archeoglobus fulgidus in the ligand free form
Analyse Crystal structure of prox from archeoglobus fulgidus in the ligand free form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SW5
- Type
- protein
- Length
- 1,080 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Osmoprotection protein (prox)
- UniProt
- O29280
- Ligands
- MG, CL
- Pockets
- 11 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Osmoprotection protein (prox) | protein | 270 | 47% helix, 19% strand | O29280 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1163 | 0.79 | 0.81 | 99 | MG |
| 2 | 675 | 0.76 | 0.82 | 74 | empty |
| 3 | 337 | 0.64 | 0.80 | 36 | empty |
| 4 | 187 | 0.47 | 0.75 | 31 | empty |
| 5 | 166 | 0.45 | 0.75 | 30 | CL |
Interfaces
5 interfaces between chains.
- B–C · 423 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 417 Ų buried · 5 hydrogen bonds · protein-protein
- A–D · 397 Ų buried · 2 hydrogen bonds · protein-protein
- C–D · 359 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 285 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 1SW5 · Crystal structure of ProX from Archeoglobus fulgidus in the ligand free form · the same entry in another collection · chain C against C, 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 O29280
- Elsewhere: RCSB PDB 1SW5 · PDBe 1SW5 · UniProt O29280
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