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T-plastin-F-actin complex

Analyse T-plastin-F-actin complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7R94
Type
protein
Length
2,570 residues
Chains
8
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Actin, alpha skeletal muscle; Plastin-3
UniProt
P68139, P13797
Ligands
ADP, MG
Pockets
20 · best druggability 0.80

Structure

electron microscopy · 2 distinct chains · 48% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
C, B, A, D, EActin, alpha skeletal muscleprotein37044% helix, 20% strandP68139
F, G, HPlastin-3protein24053% helix, 0% strandP13797

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · 5 copies · chains C, B, A, D, E
  • MG · Magnesium ion · metal · 5 copies · chains C, B, A, D, E

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

Pockets

20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111330.800.8185empty
27030.780.8376empty
33040.770.8852ADP, MG
43120.760.8849ADP, MG
52920.760.8852ADP, MG

Interfaces

13 interfaces between chains.

  • C–A · 1207 Ų buried · 10 hydrogen bonds · protein-protein
  • C–E · 1198 Ų buried · 10 hydrogen bonds · protein-protein
  • B–D · 1197 Ų buried · 10 hydrogen bonds · protein-protein
  • B–H · 892 Ų buried · 9 hydrogen bonds · protein-protein
  • C–G · 890 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 modified, 3 covalent (methylation, covalent ligand).

Compared structures

  • 7R94 · T-Plastin-F-actin complex · the same entry in another collection · chain H against H, TM-score 1.00
  • P68139 · AlphaFold monomer V2.0 prediction for actin, alpha skeletal muscle (P68139) · a predicted model of the same protein · chain D against A, TM-score 0.96

Analyse

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