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MolNFT v1 · #143051 · protein

Cryo-EM structure of F-actin complexed with the beta-III-spectrin actin-binding domain

6ANU · Actin, cytoplasmic 1: “Cryo-EM structure of F-actin complexed with the beta-III-spectrin actin-binding domain”. Electron microscopy, 20 pockets (best druggability 0.79). MolNFT v1 #143051 on GenesisL1: 3D structure, binding sites…

PDB
6ANU
Type
protein
Length
3,048 residues
Chains
12
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Actin, cytoplasmic 1; Spectrin beta chain, non-erythrocytic 2
UniProt
P60709, O15020
Pockets
20 · best druggability 0.79

Structure

electron microscopy · 2 distinct chains · 43% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
F, A, B, C, D, EActin, cytoplasmic 1protein37538% helix, 17% strandP60709
f, a, b, c, d, eSpectrin beta chain, non-erythrocytic 2protein13359% helix, 0% strandO15020

Pockets

20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17250.790.8381empty
26930.790.8482empty
36760.790.8487empty
44070.730.8345empty
53560.710.8348empty

Interfaces

19 interfaces between chains.

  • A–a · 1677 Ų buried · 42 hydrogen bonds · protein-protein
  • E–e · 1677 Ų buried · 42 hydrogen bonds · protein-protein
  • B–b · 1677 Ų buried · 42 hydrogen bonds · protein-protein
  • D–d · 1676 Ų buried · 42 hydrogen bonds · protein-protein
  • F–f · 1674 Ų buried · 42 hydrogen bonds · protein-protein

Compared structures

  • 6ANU · Cryo-EM structure of F-actin complexed with the beta-III-spectrin actin-binding domain · the same entry in another collection · chain e against e, TM-score 1.00

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