Research workbench
F1FO-ATP synthase from acinetobacter baumannii (state 3)
Analyse F1FO-ATP synthase from acinetobacter baumannii (state 3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7P3W
- Type
- protein
- Length
- 4,900 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 subunit C; ATP…
- EC
- 7.1.2.2
- UniProt
- A3M142, A3M144, A3M139, A3M137, A3M140, A3M141, A3M145, A3M143
- Ligands
- ATP, ADP, MG
- Pockets
- 20 · best druggability 0.86
Structure
electron microscopy · 13 distinct chains · 50% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP synthase subunit alpha (EC 7.1.2.2) | protein | 512 | 43% helix, 18% strand | A3M142 |
| B | ATP synthase subunit alpha (EC 7.1.2.2) | protein | 511 | 41% helix, 18% strand | A3M142 |
| C | ATP synthase subunit alpha (EC 7.1.2.2) | protein | 509 | 42% helix, 18% strand | A3M142 |
| D, F | ATP synthase subunit beta (EC 7.1.2.2) | protein | 463 | 36% helix, 19% strand | A3M144 |
| E | ATP synthase subunit beta (EC 7.1.2.2) | protein | 464 | 36% helix, 19% strand | A3M144 |
| G, H, J, O, P, S | ATP synthase subunit C | protein | 80 | 88% helix, 0% strand | A3M139 |
| K, L, Q, R | ATP synthase subunit C | protein | 79 | 86% helix, 0% strand | A3M139 |
| a | ATP synthase subunit a | protein | 277 | 68% helix, 0% strand | A3M137 |
| b | ATP synthase subunit B | protein | 150 | 88% helix, 0% strand | A3M140 |
| d | ATP synthase subunit delta | protein | 174 | 60% helix, 14% strand | A3M141 |
| e | ATP synthase epsilon chain | protein | 138 | 29% helix, 41% strand | A3M145 |
| g | ATP synthase gamma chain | protein | 288 | 60% helix, 13% strand | A3M143 |
| p | ATP synthase subunit B | protein | 155 | 97% helix, 0% strand | A3M140 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 3 copies · chains A, F, B, E, C, D
- ADP · Adenosine-5'-diphosphate · ligand · chains B, F
- MG · Magnesium ion · metal · 4 copies · chains A, B, C, 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 | 695 | 0.86 | 0.90 | 105 | MG |
| 2 | 970 | 0.86 | 0.87 | 123 | ADP, MG |
| 3 | 698 | 0.85 | 0.89 | 98 | empty |
| 4 | 735 | 0.85 | 0.89 | 104 | empty |
| 5 | 603 | 0.85 | 0.90 | 75 | ATP, MG |
Interfaces
61 interfaces between chains.
- B–F · 2612 Ų buried · 21 hydrogen bonds · protein-protein
- b–p · 2316 Ų buried · 23 hydrogen bonds · protein-protein
- A–D · 2297 Ų buried · 23 hydrogen bonds · protein-protein
- A–F · 2091 Ų buried · 20 hydrogen bonds · protein-protein
- e–g · 2035 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 7P3W · F1Fo-ATP synthase from Acinetobacter baumannii (state 3) · the same entry in another collection · chain L against L, 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 A3M142
- Every structure of UniProt A3M144
- Every structure of UniProt A3M139
- Every structure of UniProt A3M137
- Every structure of UniProt A3M140
- Every structure of UniProt A3M141
- Every structure of UniProt A3M145
- Every structure of UniProt A3M143
- Elsewhere: RCSB PDB 7P3W · PDBe 7P3W · UniProt A3M142 · UniProt A3M144 · UniProt A3M139 · UniProt A3M137 · UniProt A3M140 · UniProt A3M141 · UniProt A3M145 · UniProt A3M143
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