GL1X · GenesisL1 explorer

Research workbench

Solution structure of the CU(I) form of the yeast metallochaperone, ATX1

Analyse Solution structure of the CU(I) form of the yeast metallochaperone, ATX1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1FD8
Type
protein
Length
73 residues
Chains
1
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ATX1 copper chaperone
UniProt
P38636
Ligands
CU1

Structure

solution nmr · 1 distinct chain · 30% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AATX1 copper chaperoneprotein7330% helix, 33% strandP38636

Ligands and binding sites

  • CU1 · Copper (I) ion · metal · chains A

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

Compared structures

  • 1FD8 · Solution structure of the CU(I) form of the yeast metallochaperone, ATX1 · 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 0.90

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.