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The crystal structure of the N-terminal domain of cap indicates variable oligomerisation

Analyse The crystal structure of the N-terminal domain of cap indicates variable… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1TJF
Type
protein
Length
371 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Adenylyl cyclase-associated protein
UniProt
P54654
Ligands
SO4
Pockets
1 · best druggability 0.38

Structure

x-ray diffraction · 2 distinct chains · 74% helix, 1% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAdenylyl cyclase-associated proteinprotein18574% helix, 1% strandP54654
BAdenylyl cyclase-associated proteinprotein18675% helix, 1% strandP54654

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 6 copies · chains A, B

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11080.380.7529empty

Interfaces

1 interface between chains.

  • A–B · 484 Ų buried · 9 hydrogen bonds · protein-protein

Compared structures

  • 1TJF · The crystal structure of the N-terminal domain of CAP indicates variable oligomerisation · the same entry in another collection · chain A against A, TM-score 1.00
  • P54654 · AlphaFold monomer V2.0 prediction for adenylyl cyclase-associated protein (P54654) · a predicted model of the same protein · chain A against A, TM-score 0.98

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