Research workbench
Structural basis for VIPP1 oligomerization and maintenance of thylakoid membrane integrity
Analyse Structural basis for VIPP1 oligomerization and maintenance of thylakoid… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7O3Y
- Type
- protein
- Length
- 1,286 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.8
- Source
- Synechocystis sp. (strain PCC 6803 / Kazusa)
- Molecule
- Protein sll0617
- UniProt
- Q55707
- Ligands
- ADP
Structure
electron microscopy · resolution 3.8 · 2 distinct chains · 88% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E, F, B, D, C | Protein sll0617 | protein | 215 | 91% helix, 0% strand | Q55707 |
| A | Protein sll0617 | protein | 211 | 85% helix, 0% strand | Q55707 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
9 interfaces between chains.
- D–C · 617 Ų buried · 3 hydrogen bonds · protein-protein
- E–F · 615 Ų buried · 7 hydrogen bonds · protein-protein
- E–D · 596 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 584 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 558 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 7O3Y · Structural basis for VIPP1 oligomerization and maintenance of thylakoid membrane integrity · the same entry in another collection · chain F against F, TM-score 1.00
- Q55707 · AlphaFold monomer V2.0 prediction for protein SLL0617 (Q55707) · a predicted model of the same protein · chain E against A, TM-score 0.71
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 Q55707
- Elsewhere: RCSB PDB 7O3Y · PDBe 7O3Y · UniProt Q55707
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