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Model of actin-fimbrin ABD2 complex

Analyse Model of actin-fimbrin ABD2 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3BYH
Type
protein
Length
605 residues
Chains
2
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Actin; Fimbrin ABD2
UniProt
Q1KLZ0
Pockets
6 · best druggability 0.76

Structure

electron microscopy · 2 distinct chains · 48% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AActinprotein37440% helix, 20% strandQ1KLZ0
BFimbrin ABD2protein23161% helix, 0% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17660.760.8081empty
26570.680.7649empty
32510.580.7940empty
41440.510.7926empty
51270.440.7618empty

Interfaces

1 interface between chains.

  • A–B · 949 Ų buried · 47 hydrogen bonds · protein-protein

Compared structures

  • 3BYH · Model of actin-fimbrin ABD2 complex · the same entry in another collection · chain A against A, TM-score 1.00

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