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Crystal structure of the archaeal secretion ATPase gspe in complex with phosphate
Analyse Crystal structure of the archaeal secretion ATPase gspe in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OAQ
- Type
- protein
- Length
- 1,001 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Type II secretion system protein
- UniProt
- O29598
- Ligands
- PO4
- Pockets
- 10 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| 1 | Type II secretion system protein | protein | 498 | 35% helix, 23% strand | O29598 |
| 2 | Type II secretion system protein | protein | 503 | 38% helix, 23% strand | O29598 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 4 copies · chains 1, 2
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 829 | 0.81 | 0.84 | 77 | PO4 |
| 2 | 896 | 0.76 | 0.80 | 85 | PO4 |
| 3 | 289 | 0.65 | 0.82 | 30 | empty |
| 4 | 181 | 0.50 | 0.77 | 25 | empty |
| 5 | 237 | 0.50 | 0.75 | 31 | empty |
Interfaces
1 interface between chains.
- 1–2 · 2112 Ų buried · 34 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 33 modified (engineered).
Compared structures
- 2OAQ · Crystal structure of the archaeal secretion ATPase GspE in complex with phosphate · the same entry in another collection · chain 1 against 1, 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 O29598
- Elsewhere: RCSB PDB 2OAQ · PDBe 2OAQ · UniProt O29598
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