Research workbench
Microscopic rotary mechanism of ion translocation in the fo complex of ATP synthases
Analyse Microscopic rotary mechanism of ion translocation in the fo complex of ATP… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XQS
- Type
- protein
- Length
- 410 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP synthase C chain
- UniProt
- D5A0Q7
- Ligands
- CVM
Structure
x-ray diffraction · 1 distinct chain · 85% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | ATP synthase C chain | protein | 82 | 85% helix, 0% strand | D5A0Q7 |
Ligands and binding sites
- CVM · Cymal-4 · ligand · 40 copies · chains A, B, C, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
4 interfaces between chains.
- B–C · 1935 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 1927 Ų buried · 11 hydrogen bonds · protein-protein
- C–D · 1912 Ų buried · 12 hydrogen bonds · protein-protein
- D–E · 1882 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 modified (formylation).
Compared structures
- 2XQS · Microscopic rotary mechanism of ion translocation in the Fo complex of ATP synthases · 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 D5A0Q7
- Elsewhere: RCSB PDB 2XQS · PDBe 2XQS · UniProt D5A0Q7
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