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Actin filament model in the extended form of acromsomal bundle in the limulus sperm

Analyse Actin filament model in the extended form of acromsomal bundle in the limulus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3B63
Type
protein
Length
5,093 residues
Chains
14
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Actin
Pockets
20 · best druggability 0.86

Structure

electron microscopy · 7 distinct chains · 41% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, GActinprotein36541% helix, 20% strand—
BActinprotein36442% helix, 20% strand—
C, IActinprotein36543% helix, 20% strand—
DActinprotein35739% helix, 18% strand—
E, H, J, K, NActinprotein36542% helix, 19% strand—
FActinprotein35741% helix, 19% strand—
L, MActinprotein36537% helix, 20% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110060.860.87139empty
211620.820.83135empty
310250.810.82105empty
411830.790.8198empty
52620.790.9158empty

Interfaces

25 interfaces between chains.

  • I–J · 1187 Ų buried · 32 hydrogen bonds · protein-protein
  • M–N · 1120 Ų buried · 11 hydrogen bonds · protein-protein
  • L–M · 1085 Ų buried · 13 hydrogen bonds · protein-protein
  • K–L · 1061 Ų buried · 30 hydrogen bonds · protein-protein
  • E–F · 989 Ų buried · 16 hydrogen bonds · protein-protein

Compared structures

  • 3B63 · Actin filament model in the extended form of acromsomal bundle in the Limulus sperm · the same entry in another collection · chain E against E, TM-score 1.00

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