MolNFT v1 · #163334 · protein
Structure of S-MGM1 decorating the inner surface of tubulated lipid membranes in the gtpgammas bound state
6RZW · Putative mitochondrial dynamin protein: “Structure of S-MGM1 decorating the inner surface of tubulated lipid membranes in the gtpgammas bound state”. Electron microscopy, 20 pockets (best druggability 0.83). MolNFT v1 #163334 on…
- PDB
- 6RZW
- Type
- protein
- Length
- 6,590 residues
- Chains
- 10
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative mitochondrial dynamin protein
- UniProt
- G0SGC7
- Pockets
- 20 · best druggability 0.83
Structure
electron microscopy · 1 distinct chain · 64% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J | Putative mitochondrial dynamin protein | protein | 659 | 64% helix, 7% strand | G0SGC7 |
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 | 270 | 0.83 | 0.94 | 66 | empty |
| 2 | 149 | 0.75 | 0.93 | 48 | empty |
| 3 | 162 | 0.74 | 0.91 | 45 | empty |
| 4 | 68 | 0.74 | 0.98 | 27 | empty |
| 5 | 759 | 0.74 | 0.79 | 69 | empty |
Interfaces
16 interfaces between chains.
- E–F · 659 Ų buried · 3 hydrogen bonds · protein-protein
- I–J · 657 Ų buried · 2 hydrogen bonds · protein-protein
- C–D · 656 Ų buried · 2 hydrogen bonds · protein-protein
- G–H · 647 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 645 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 disulfide (disulfide).
Compared structures
- 6RZW · Structure of s-Mgm1 decorating the inner surface of tubulated lipid membranes in the… · the same entry in another collection · chain A against A, 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 G0SGC7
- Elsewhere: RCSB PDB 6RZW · PDBe 6RZW · UniProt G0SGC7
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