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Structural insights into G domain dimerization and pathogenic mutations of OPA1

Analyse Structural insights into G domain dimerization and pathogenic mutations of OPA1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6JTG
Type
protein
Length
330 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Dynamin-like 120 kda protein, MITOCHONDRIAL,OPA1 protein
EC
3.6.5.5
UniProt
O60313, Q6PEK6
Ligands
GDP, BEF, MG, K
Pockets
4 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ADynamin-like 120 kda protein, MITOCHONDRIAL,OPA1 protein (EC 3.6.5.5)protein33042% helix, 15% strandO60313, Q6PEK6

Ligands and binding sites

  • GDP · Guanosine-5'-diphosphate · ligand · chains A
  • BEF · Beryllium trifluoride ion · ligand · chains A
  • MG · Magnesium ion · metal · chains A
  • K · Potassium ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11660.660.8733GDP, MG, BEF, K
22730.570.7738empty
3520.440.8415empty
4970.390.7625empty

Compared structures

  • 6JTG · Structural insights into G domain dimerization and pathogenic mutations of OPA1 · the same entry in another collection · chain A against A, TM-score 1.00
  • O60313 · AlphaFold monomer V2.0 prediction for dynamin-like 120 kda protein, mitochondrial (O60313) · a predicted model of the same protein · chain A against A, TM-score 0.96

Analyse

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