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Structure of the PHACTR1 rpel-2 bound to G-actin

Analyse Structure of the PHACTR1 rpel-2 bound to G-actin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4B1X
Type
protein
Length
385 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Actin, alpha skeletal muscle; Phosphatase and actin regulator 1
UniProt
P68135, G5E8P7
Ligands
LAB, ATP, MG
Pockets
2 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
BActin, alpha skeletal muscleprotein35745% helix, 20% strandP68135
MPhosphatase and actin regulator 1protein2857% helix, 0% strandG5E8P7

Ligands and binding sites

  • LAB · Latrunculin B · ligand · chains B
  • ATP · Adenosine-5'-triphosphate · ligand · chains B
  • MG · Magnesium ion · metal · chains B

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13610.720.8447LAB, ATP, MG
22630.610.8041empty

Interfaces

1 interface between chains.

  • B–M · 984 Ų buried · 13 hydrogen bonds · protein-protein

Compared structures

  • 4B1X · Structure of the Phactr1 RPEL-2 bound to G-actin · the same entry in another collection · chain B against B, TM-score 1.00
  • P68135 · AlphaFold monomer V2.0 prediction for actin, alpha skeletal muscle (P68135) · a predicted model of the same protein · chain B against A, TM-score 0.99

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