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Dynamin 1 GTPase dimer, short axis form

Analyse Dynamin 1 GTPase dimer, short axis form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2X2F
Type
protein
Length
669 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Dynamin-1
EC
3.6.5.5
UniProt
Q05193
Ligands
GDP, ALF, MG, NA
Pockets
7 · best druggability 0.87

Structure

x-ray diffraction · 2 distinct chains · 47% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ADynamin-1 (EC 3.6.5.5)protein33648% helix, 14% strandQ05193
DDynamin-1 (EC 3.6.5.5)protein33346% helix, 14% strandQ05193

Ligands and binding sites

  • GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, D
  • ALF · Tetrafluoroaluminate ion · ligand · 2 copies · chains A, D
  • MG · Magnesium ion · metal · 2 copies · chains A, D
  • NA · Sodium ion · metal · 2 copies · chains A, D

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17990.870.90114GDP, ALF, MG, NA
22370.580.7928empty
3570.450.8413empty
4880.370.7622empty
5540.300.7616empty

Interfaces

1 interface between chains.

  • A–D · 1495 Ų buried · 23 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 modified (engineered).

Compared structures

  • 2X2F · Dynamin 1 GTPase dimer, short axis form · the same entry in another collection · chain A against A, TM-score 1.00
  • Q05193 · AlphaFold monomer V2.0 prediction for dynamin-1 (Q05193) · a predicted model of the same protein · chain D against A, TM-score 0.92

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