Research workbench
Cryo-EM structure of the mammalian dp-state ATP synthase fo section
Analyse Cryo-EM structure of the mammalian dp-state ATP synthase fo section in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6J5A
- Type
- protein
- Length
- 1,282 residues
- Chains
- 18
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP synthase peripheral stalk-membrane subunit B; ATP synthase subunit D, mitochondrial…
- UniProt
- A0A286ZYM6, A0A287B4I0, Q95339, F1RFD4, Q35914, Q35915, Q4VT52
- Pockets
- 13 · best druggability 0.85
Structure
electron microscopy · 11 distinct chains · 60% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| b | ATP synthase peripheral stalk-membrane subunit B | protein | 82 | 72% helix, 0% strand | A0A286ZYM6 |
| d | ATP synthase subunit D, mitochondrial | protein | 24 | 13% helix, 0% strand | A0A287B4I0 |
| e | ATP synthase subunit E, mitochondrial | protein | 63 | 90% helix, 0% strand | — |
| f | ATP synthase subunit F, mitochondrial | protein | 87 | 49% helix, 0% strand | Q95339 |
| g | ATP synthase subunit G, mitochondrial | protein | 84 | 61% helix, 0% strand | — |
| i | ATP synthase membrane subunit dapit | protein | 42 | 74% helix, 0% strand | F1RFD4 |
| k | Subunit K analog | protein | 29 | 55% helix, 0% strand | — |
| 8 | ATP synthase protein 8 | protein | 30 | 37% helix, 0% strand | Q35914 |
| a | ATP synthase subunit a | protein | 223 | 49% helix, 0% strand | Q35915 |
| K, L, M, N, O, P, Q, R | Mitochondrial H+ transporting ATP synthase subunit C isoform 1 | protein | 72 | 85% helix, 0% strand | Q4VT52 |
| u | ATP synthase membrane subunit 6.8PL | protein | 42 | 55% helix, 0% strand | — |
Pockets
13 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1094 | 0.85 | 0.85 | 97 | empty |
| 2 | 833 | 0.84 | 0.86 | 85 | empty |
| 3 | 357 | 0.80 | 0.89 | 47 | empty |
| 4 | 552 | 0.73 | 0.81 | 56 | empty |
| 5 | 562 | 0.73 | 0.81 | 69 | empty |
Interfaces
37 interfaces between chains.
- Q–R · 1517 Ų buried · 2 hydrogen bonds · protein-protein
- M–N · 1514 Ų buried · 9 hydrogen bonds · protein-protein
- N–O · 1497 Ų buried · 12 hydrogen bonds · protein-protein
- K–R · 1443 Ų buried · 3 hydrogen bonds · protein-protein
- K–L · 1441 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 6J5A · Cryo-EM structure of the mammalian DP-state ATP synthase FO section · the same entry in another collection · chain u against u, 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 A0A286ZYM6
- Every structure of UniProt A0A287B4I0
- Every structure of UniProt Q95339
- Every structure of UniProt F1RFD4
- Every structure of UniProt Q35914
- Every structure of UniProt Q35915
- Every structure of UniProt Q4VT52
- Elsewhere: RCSB PDB 6J5A · PDBe 6J5A · UniProt A0A286ZYM6 · UniProt A0A287B4I0 · UniProt Q95339 · UniProt F1RFD4 · UniProt Q35914 · UniProt Q35915 · UniProt Q4VT52
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