Research workbench
Autoinhibited E. COLI ATP synthase state 1
Analyse Autoinhibited E. COLI ATP synthase state 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5T4O
- Type
- protein
- Length
- 4,778 residues
- Chains
- 22
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP synthase subunit alpha; ATP synthase subunit beta; ATP synthase gamma chain; ATP…
- EC
- 3.6.3.14
- UniProt
- B7MGF4, B7MGF2, B7MGF3, B7MGF1, P0ABA2, B7L888, B7MGF5, B7NR39
- Ligands
- ATP, ADP
- Pockets
- 20 · best druggability 0.81
Structure
electron microscopy · 10 distinct chains · 47% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP synthase subunit alpha (EC 3.6.3.14) | protein | 511 | 39% helix, 10% strand | B7MGF4 |
| B | ATP synthase subunit alpha (EC 3.6.3.14) | protein | 510 | 35% helix, 10% strand | B7MGF4 |
| C | ATP synthase subunit alpha (EC 3.6.3.14) | protein | 508 | 37% helix, 10% strand | B7MGF4 |
| D, E, F | ATP synthase subunit beta (EC 3.6.3.14) | protein | 466 | 36% helix, 12% strand | B7MGF2 |
| G | ATP synthase gamma chain | protein | 284 | 60% helix, 7% strand | B7MGF3 |
| H | ATP synthase epsilon chain | protein | 136 | 22% helix, 29% strand | B7MGF1 |
| I, J | ATP synthase subunit B | protein | 155 | 89% helix, 0% strand | P0ABA2 |
| K | ATP synthase subunit a | protein | 211 | 82% helix, 0% strand | B7L888 |
| L | ATP synthase subunit delta | protein | 160 | 66% helix, 0% strand | B7MGF5 |
| M, N, O, P, Q, R, S, T, U, V | ATP synthase subunit C | protein | 75 | 96% helix, 0% strand | B7NR39 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 3 copies · chains A, B, C
- ADP · Adenosine-5'-diphosphate · ligand · chains B, F
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 | 792 | 0.81 | 0.85 | 115 | empty |
| 2 | 820 | 0.81 | 0.84 | 122 | empty |
| 3 | 836 | 0.81 | 0.84 | 119 | empty |
| 4 | 981 | 0.78 | 0.81 | 118 | empty |
| 5 | 735 | 0.78 | 0.83 | 116 | empty |
Interfaces
37 interfaces between chains.
- I–J · 952 Ų buried · 0 hydrogen bonds · protein-protein
- M–V · 796 Ų buried · 2 hydrogen bonds · protein-protein
- Q–R · 794 Ų buried · 2 hydrogen bonds · protein-protein
- O–P · 792 Ų buried · 2 hydrogen bonds · protein-protein
- R–S · 789 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 5T4O · Autoinhibited E. coli ATP synthase state 1 · the same entry in another collection · chain J against J, 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 B7MGF4
- Every structure of UniProt B7MGF2
- Every structure of UniProt B7MGF3
- Every structure of UniProt B7MGF1
- Every structure of UniProt P0ABA2
- Every structure of UniProt B7L888
- Every structure of UniProt B7MGF5
- Every structure of UniProt B7NR39
- Elsewhere: RCSB PDB 5T4O · PDBe 5T4O · UniProt B7MGF4 · UniProt B7MGF2 · UniProt B7MGF3 · UniProt B7MGF1 · UniProt P0ABA2 · UniProt B7L888 · UniProt B7MGF5 · UniProt B7NR39
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.