MolNFT v1 · #54497 · protein
Microscopic rotary mechanism of ion translocation in the fo complex of ATP synthases
2XQS · ATP synthase C chain: “Microscopic rotary mechanism of ion translocation in the fo complex of ATP synthases”. X-ray diffraction, 1 ligand (CVM). MolNFT v1 #54497 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- 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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