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The structure of F1-ATPase inhibited by quercetin.
Analyse The structure of F1-ATPase inhibited by quercetin. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2JJ2
- Type
- protein
- Length
- 6,054 residues
- Chains
- 14
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP synthase subunit alpha heart isoform; ATP synthase subunit beta; ATP synthase gamma…
- EC
- 3.6.1.34
- UniProt
- P19483, P00829, P05631
- Ligands
- ANP, ADP, QUE, MG, AZI, PO4
- Pockets
- 20 · best druggability 0.90
Structure
x-ray diffraction · 6 distinct chains · 43% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, H | ATP synthase subunit alpha heart isoform (EC 3.6.1.34) | protein | 487 | 43% helix, 20% strand | P19483 |
| B, I | ATP synthase subunit alpha heart isoform (EC 3.6.1.34) | protein | 479 | 41% helix, 21% strand | P19483 |
| C, J | ATP synthase subunit alpha heart isoform (EC 3.6.1.34) | protein | 495 | 42% helix, 20% strand | P19483 |
| D, K | ATP synthase subunit beta (EC 3.6.1.34) | protein | 467 | 38% helix, 21% strand | P00829 |
| E, F, L, M | ATP synthase subunit beta (EC 3.6.1.34) | protein | 466 | 40% helix, 21% strand | P00829 |
| G, N | ATP synthase gamma chain (EC 3.6.1.34) | protein | 167 | 71% helix, 2% strand | P05631 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 8 copies · chains A, D, B, E, C, F, H, K, I, L, J, M
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains C, D, J, K
- QUE · 3,5,7,3',4'-pentahydroxyflavone · ligand · 2 copies · chains B, C, F, G, I, J, M, N
- MG · Magnesium ion · metal · 10 copies · chains A, B, C, D, F, H, I, J, K, M
- AZI · Azide ion · ion · 2 copies · chains C, D, J, K
- PO4 · Phosphate ion · ion · 2 copies · chains E, L
- GOL · Glycerol · additive · 12 copies · chains A, E, B, F, C, D, H, L, I, J, K
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1118 | 0.90 | 0.91 | 155 | ANP, MG, QUE |
| 2 | 802 | 0.88 | 0.91 | 90 | ANP, MG |
| 3 | 764 | 0.87 | 0.91 | 99 | ANP, MG, QUE |
| 4 | 1086 | 0.87 | 0.88 | 122 | GOL |
| 5 | 723 | 0.87 | 0.91 | 93 | ANP, MG |
Interfaces
29 interfaces between chains.
- J–K · 3090 Ų buried · 45 hydrogen bonds · protein-protein
- C–D · 3089 Ų buried · 46 hydrogen bonds · protein-protein
- H–K · 2613 Ų buried · 29 hydrogen bonds · protein-protein
- A–D · 2607 Ų buried · 27 hydrogen bonds · protein-protein
- J–M · 2428 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
- 2JJ2 · The Structure of F1-ATPase inhibited by quercetin. · the same entry in another collection · chain H against H, 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 P19483
- Every structure of UniProt P00829
- Every structure of UniProt P05631
- Elsewhere: RCSB PDB 2JJ2 · PDBe 2JJ2 · UniProt P19483 · UniProt P00829 · UniProt P05631
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