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Structure of homodimeric actin capping protein alpha subunit from plasmodium berghei

Analyse Structure of homodimeric actin capping protein alpha subunit from plasmodium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7A0H
Type
protein
Length
540 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
F-actin-capping protein subunit alpha
UniProt
A0A509AR49
Ligands
BR
Pockets
12 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AF-actin-capping protein subunit alphaprotein28535% helix, 38% strandA0A509AR49
BF-actin-capping protein subunit alphaprotein25540% helix, 34% strandA0A509AR49

Ligands and binding sites

  • BR · Bromide ion · ion · 25 copies · chains A, B
  • GOL · Glycerol · additive · chains A
  • EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12400.740.8832BR
23510.620.7845empty
32180.590.8136empty
41300.510.8017BR
5760.490.8320empty

Interfaces

1 interface between chains.

  • A–B · 2314 Ų buried · 19 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 7A0H · Structure of homodimeric actin capping protein alpha subunit from Plasmodium berghei · the same entry in another collection · chain A against A, TM-score 1.00

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