GL1X · GenesisL1 explorer

Research workbench

Bound structure of CRF1 extracellular domain antagonist

Analyse Bound structure of CRF1 extracellular domain antagonist in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2O8Z
Type
protein
Length
12 residues
Chains
1
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
CCRF(30-41) peptide
Ligands
ACE, NH2

Structure

solution nmr · 1 distinct chain · 83% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACCRF(30-41) peptideprotein1283% helix, 0% strand—

Ligands and binding sites

  • ACE · Acetyl group · ligand · chains A
  • NH2 · Amino group · ion · 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

  • 2O8Z · Bound Structure of CRF1 Extracellular Domain Antagonist · 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.