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MolNFT v1 · #148962 · protein

Carp domain of mouse cyclase-associated protein 1 (CAP1) bound to ADP- actin

6FM2 · Actin, alpha skeletal muscle: “Carp domain of mouse cyclase-associated protein 1 (CAP1) bound to ADP- actin”. X-ray diffraction, 2 ligands (ADP, MG), 2 pockets (best druggability 0.76). MolNFT v1 #148962 on GenesisL1: 3D structure…

PDB
6FM2
Type
protein
Length
528 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Actin, alpha skeletal muscle; Adenylyl cyclase-associated protein 1
UniProt
P68135, P40124
Ligands
ADP, MG
Pockets
2 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 31% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AActin, alpha skeletal muscleprotein37143% helix, 19% strandP68135
BAdenylyl cyclase-associated protein 1protein1572% helix, 58% strandP40124

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · chains A
  • MG · Magnesium ion · metal · chains A

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
15660.760.8258empty
24030.730.8454MG, ADP

Interfaces

1 interface between chains.

  • A–B · 991 Ų buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (methylation).

Compared structures

  • 6FM2 · CARP domain of mouse cyclase-associated protein 1 (CAP1) bound to ADP-actin · the same entry in another collection · chain A against A, TM-score 1.00
  • P40124 · AlphaFold monomer V2.0 prediction for adenylyl cyclase-associated protein 1 (P40124) · a predicted model of the same protein · chain B against A, TM-score 0.98
  • P68135 · AlphaFold monomer V2.0 prediction for actin, alpha skeletal muscle (P68135) · a predicted model of the same protein · chain A against A, TM-score 0.92

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