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X-ray structure of bistramide a- actin complex at 1.35 a resolution.

Analyse X-ray structure of bistramide a- actin complex at 1.35 a resolution. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2FXU
Type
protein
Length
361 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Actin, alpha skeletal muscle
UniProt
P68135
Ligands
ATP, BID, CA
Pockets
3 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AActin, alpha skeletal muscleprotein36144% helix, 20% strandP68135

Ligands and binding sites

  • ATP · Adenosine-5'-triphosphate · ligand · chains A
  • BID · Bistramide A · ligand · chains A
  • CA · Calcium ion · metal · 4 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13320.740.8645CA, ATP
21150.420.7620BID
3610.310.7611empty

Modifications

Observed in the structure: 1 modified (methylation).

Compared structures

  • 2FXU · X-ray Structure of Bistramide A- Actin Complex at 1.35 A resolution. · the same entry in another collection · chain A against A, TM-score 1.00
  • P68135 · AlphaFold monomer V2.0 prediction for actin, alpha skeletal muscle (P68135) · a predicted model of the same protein · chain A against A, TM-score 0.98

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