Research workbench
Crystal structure of a mycobacterial ATP synthase rotor ring in complex with iodo-bedaquiline
Analyse Crystal structure of a mycobacterial ATP synthase rotor ring 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
- 4V1H
- Type
- protein
- Length
- 255 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- F0F1 ATP synthase subunit C
- EC
- 3.6.3.14
- UniProt
- I0RTF3
- Ligands
- IBQ, TAM
Structure
x-ray diffraction · 1 distinct chain · 87% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | F0F1 ATP synthase subunit C (EC 3.6.3.14) | protein | 85 | 87% helix, 0% strand | I0RTF3 |
Ligands and binding sites
- IBQ · Iodo-bedaquiline · ligand · 3 copies · chains A, B, C
- TAM · Tris(hydroxyethyl)aminomethane · ligand · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
2 interfaces between chains.
- B–C · 1792 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 1729 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 4V1H · Crystal structure of a mycobacterial ATP synthase rotor ring in complex with… · 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 I0RTF3
- Elsewhere: RCSB PDB 4V1H · PDBe 4V1H · UniProt I0RTF3
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