Research workbench
Structure of the 6TH orf of the rhodobacter blastica ATPase operon; majastridin
Analyse Structure of the 6TH orf of the rhodobacter blastica ATPase operon; majastridin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2NXV
- Type
- protein
- Length
- 498 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP synthase subunits region orf 6
- UniProt
- P05449
- Pockets
- 7 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | ATP synthase subunits region orf 6 | protein | 249 | 26% helix, 29% strand | P05449 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 140 | 0.78 | 0.95 | 21 | empty |
| 2 | 406 | 0.70 | 0.81 | 42 | GOL |
| 3 | 495 | 0.68 | 0.79 | 40 | GOL |
| 4 | 149 | 0.45 | 0.76 | 29 | empty |
| 5 | 142 | 0.41 | 0.74 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 2273 Ų buried · 34 hydrogen bonds · protein-protein
Compared structures
- 2NXV · Structure of the 6th ORF of the Rhodobacter blastica ATPase operon; Majastridin · the same entry in another collection · chain A against A, TM-score 1.00
- P05449 · AlphaFold monomer V2.0 prediction for ATP synthase subunits region orf 6 (P05449) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P05449
- Elsewhere: RCSB PDB 2NXV · PDBe 2NXV · UniProt P05449
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