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Structure of S-MGM1 decorating the inner surface of tubulated lipid membranes

Analyse Structure of S-MGM1 decorating the inner surface of tubulated lipid membranes in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6RZV
Type
protein
Length
10,544 residues
Chains
16
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Putative mitochondrial dynamin protein
UniProt
G0SGC7
Pockets
20 · best druggability 0.80

Structure

electron microscopy · 1 distinct chain · 63% helix, 7% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, PPutative mitochondrial dynamin proteinprotein65963% helix, 7% strandG0SGC7

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12320.800.9357empty
22370.800.9359empty
31480.780.9548empty
4840.740.9620empty
5970.740.9525empty

Interfaces

30 interfaces between chains.

  • E–J · 1393 Ų buried · 110 hydrogen bonds · protein-protein
  • G–L · 1055 Ų buried · 47 hydrogen bonds · protein-protein
  • E–F · 658 Ų buried · 3 hydrogen bonds · protein-protein
  • I–J · 658 Ų buried · 3 hydrogen bonds · protein-protein
  • C–D · 655 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 disulfide, 1 isopeptide (disulfide, isopeptide).

Compared structures

  • 6RZV · Structure of s-Mgm1 decorating the inner surface of tubulated lipid membranes · the same entry in another collection · chain A against A, TM-score 1.00

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