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Crystal structure of the ATX1 metallochaperone protein

Analyse Crystal structure of the ATX1 metallochaperone protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1CC7
Type
protein
Length
72 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein (metallochaperone ATX1)
UniProt
P38636
Ligands
BEN

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein (metallochaperone ATX1)protein7226% helix, 36% strandP38636

Ligands and binding sites

  • BEN · Benzamidine · ligand · chains A

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

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 1CC7 · Crystal structure of the ATX1 metallochaperone protein · the same entry in another collection · chain A against A, TM-score 1.00
  • P38636 · AlphaFold monomer V2.0 prediction for metal homeostasis factor ATX1 (P38636) · a predicted model of the same protein · chain A against A, TM-score 0.95

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