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Structure of cyclic peptide inhibitors of mammalian ribonucleotide reductase

Analyse Structure of cyclic peptide inhibitors of mammalian ribonucleotide reductase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1FOZ
Type
protein
Length
7 residues
Chains
1
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Synthetic cyclic peptide
Ligands
ACE

Structure

solution nmr · 1 distinct chain · 0% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASynthetic cyclic peptideprotein70% helix, 0% strand—

Ligands and binding sites

  • ACE · Acetyl group · ligand · chains A

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

Modifications

Observed in the structure: 1 covalent, 1 isopeptide (covalent ligand, isopeptide).

Compared structures

  • 1FOZ · Structure of cyclic peptide inhibitors of mammalian ribonucleotide reductase · the same entry in another collection · chain A against A, TM-score 1.00

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