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Structure of a molybdopterin-bound CNX1G domain links molybdenum and copper metabolism

Analyse Structure of a molybdopterin-bound CNX1G domain links molybdenum and copper… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1UUX
Type
protein
Length
161 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Molybdopterin biosynthesis CNX1
UniProt
Q39054
Ligands
MTE, CU1
Pockets
1 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMolybdopterin biosynthesis CNX1protein16148% helix, 21% strandQ39054

Ligands and binding sites

  • MTE · Phosphonic acidmono-(2-amino-5,6-dimercapto-4-oxo-3,7,8A,9,10,10A-hexahydro-4H-8-oxa-1,3,9,10-tetraaza-anthracen-7-ylmethyl)ester · ligand · chains A
  • CU1 · Copper (I) ion · metal · chains A
  • PPI · Propanoic acid · additive · chains A
  • IMD · Imidazole · additive · chains A
  • FMT · Formic acid · additive · 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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11640.510.7835MTE

Compared structures

  • 1UUX · Structure of a molybdopterin-bound cnx1g domain links molybdenum and copper metabolism · the same entry in another collection · chain A against A, TM-score 1.00
  • Q39054 · AlphaFold monomer V2.0 prediction for molybdopterin biosynthesis protein CNX1 (Q39054) · a predicted model of the same protein · chain A against A, TM-score 0.99

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