GL1X · GenesisL1 explorer

Research workbench

Switching the chirality of the metal environment alters the coordination mode in designed peptides.

Analyse Switching the chirality of the metal environment alters the coordination mode… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3H5F
Type
protein
Length
87 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Coil ser L16L-pen
Ligands
ACE, ZN, NH2, CL

Structure

x-ray diffraction · 1 distinct chain · 90% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CCoil ser L16L-penprotein2990% helix, 0% strand—

Ligands and binding sites

  • ACE · Acetyl group · ligand · 3 copies · chains A, B, C
  • ZN · Zinc ion · metal · 4 copies · chains A, C
  • NH2 · Amino group · ion · 3 copies · chains A, B, C
  • CL · Chloride ion · ion · 3 copies · chains A, B, C
  • ACT · Acetate ion · additive · chains B, C

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

Interfaces

3 interfaces between chains.

  • A–C · 613 Ų buried · 5 hydrogen bonds · protein-protein
  • B–C · 612 Ų buried · 2 hydrogen bonds · protein-protein
  • A–B · 542 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 3 covalent, 3 modified (covalent ligand, nonstandard).

Compared structures

  • 3H5F · Switching the Chirality of the Metal Environment Alters the Coordination Mode in Designed… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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