X-ray crystallographic analyses of symmetrical allosteric effectors of hemoglobin. compounds designed to link primary and secondary binding sites

Structure

x-ray diffraction · 2 distinct chains · 78% helix, 0% strand (DSSP).

Ligands and binding sites

• HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, B, C, D
• CNO · 2-{4-[(3{2-[4-(1-carboxy-1-methyl-ethoxy)-phenyl]-acetylamino}-phenylcarbamoyl)-methyl]-phenoxy}-2-methyl-propionic acid · ligand · 2 copies · chains A, B, C, D
• SO4 · Sulfate ion · ion · 2 copies · chains B, D

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

Pockets

10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Interfaces

5 interfaces between chains.

• A–B · 850 Ų buried · 10 hydrogen bonds · protein-protein
• C–D · 845 Ų buried · 10 hydrogen bonds · protein-protein
• A–D · 721 Ų buried · 10 hydrogen bonds · protein-protein
• B–C · 674 Ų buried · 7 hydrogen bonds · protein-protein
• A–C · 318 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

• 1K0Y · X-ray Crystallographic Analyses of Symmetrical Allosteric Effectors of Hemoglobin.… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt P69905
• Every structure of UniProt P68871
• Elsewhere: RCSB PDB 1K0Y · PDBe 1K0Y · UniProt P69905 · UniProt P68871