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Crystal structure of the bateman domain of murine magnesium transporter CNNM2 bound to AMP

Analyse Crystal structure of the bateman domain of murine magnesium transporter CNNM2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4P1G
Type
protein
Length
152 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Metal transporter CNNM2
UniProt
Q3TWN3
Ligands
AMP
Pockets
1 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMetal transporter CNNM2protein15239% helix, 27% strandQ3TWN3

Ligands and binding sites

  • AMP · Adenosine monophosphate · ligand · chains A

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
1580.360.7913AMP

Compared structures

  • 4P1G · Crystal structure of the Bateman domain of murine magnesium transporter CNNM2 bound to AMP · the same entry in another collection · chain A against A, TM-score 1.00
  • Q3TWN3 · AlphaFold monomer V2.0 prediction for metal transporter CNNM2 (Q3TWN3) · a predicted model of the same protein · chain A against A, TM-score 0.97

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