Research workbench
Bovine ATP synthase stator domain, state 3
Analyse Bovine ATP synthase stator domain, state 3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ZIU
- Type
- protein
- Length
- 1,162 residues
- Chains
- 11
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP synthase protein 8; ATP synthase subunit a; ATP synthase subunit D, mitochondrial…
- UniProt
- P03929, P00847, P13620, Q00361, Q28851, Q28852, P14790, P13619, P02721, P13621, P19483
- Pockets
- 20 · best druggability 0.78
Structure
electron microscopy · 11 distinct chains · 65% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| 8 | ATP synthase protein 8 | protein | 41 | 66% helix, 0% strand | P03929 |
| a | ATP synthase subunit a | protein | 226 | 76% helix, 0% strand | P00847 |
| d | ATP synthase subunit D, mitochondrial | protein | 155 | 57% helix, 1% strand | P13620 |
| e | ATP synthase subunit E, mitochondrial | protein | 41 | 83% helix, 0% strand | Q00361 |
| f | ATP synthase subunit F, mitochondrial | protein | 83 | 55% helix, 1% strand | Q28851 |
| g | ATP synthase subunit G, mitochondrial | protein | 79 | 77% helix, 1% strand | Q28852 |
| j | ATP synthase subunit ATP5MPL, mitochondrial | protein | 48 | 83% helix, 0% strand | P14790 |
| b | ATP synthase F(0) complex subunit B1, mitochondrial | protein | 209 | 83% helix, 2% strand | P13619 |
| h | ATP synthase-coupling factor 6, mitochondrial | protein | 62 | 56% helix, 0% strand | P02721 |
| S | ATP synthase subunit O, mitochondrial | protein | 129 | 53% helix, 16% strand | P13621 |
| C | ATP synthase subunit alpha, mitochondrial | protein | 89 | 12% helix, 38% strand | P19483 |
Pockets
20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 942 | 0.78 | 0.79 | 75 | empty |
| 2 | 301 | 0.74 | 0.87 | 50 | empty |
| 3 | 331 | 0.72 | 0.84 | 46 | empty |
| 4 | 131 | 0.67 | 0.88 | 28 | empty |
| 5 | 329 | 0.62 | 0.79 | 47 | empty |
Interfaces
23 interfaces between chains.
- d–b · 3004 Ų buried · 29 hydrogen bonds · protein-protein
- 8–a · 1371 Ų buried · 5 hydrogen bonds · protein-protein
- b–h · 1343 Ų buried · 16 hydrogen bonds · protein-protein
- a–b · 1119 Ų buried · 8 hydrogen bonds · protein-protein
- a–f · 1036 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
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 P03929
- Every structure of UniProt P00847
- Every structure of UniProt P13620
- Every structure of UniProt Q00361
- Every structure of UniProt Q28851
- Every structure of UniProt Q28852
- Every structure of UniProt P14790
- Every structure of UniProt P13619
- Every structure of UniProt P02721
- Every structure of UniProt P13621
- Every structure of UniProt P19483
- Elsewhere: RCSB PDB 6ZIU · PDBe 6ZIU · UniProt P03929 · UniProt P00847 · UniProt P13620 · UniProt Q00361 · UniProt Q28851 · UniProt Q28852 · UniProt P14790 · UniProt P13619 · UniProt P02721 · UniProt P13621 · UniProt P19483
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