Crystal structure of ferric R-state human methemoglobin bound to maleimide-deferoxamine bifunctional chelator (dfo)

Structure

x-ray diffraction · 2 distinct chains · 82% helix, 0% strand (DSSP).

Ligands and binding sites

• HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, B, C, D
• G7Z · 3-[2,5-bis(oxidanylidene)pyrrolidin-1-yl]-~{N}-methyl-propanamide · ligand · 2 copies · chains B, D
• SO4 · Sulfate ion · ion · 7 copies · chains A, D, B, C
• OXY · Oxygen molecule · ion · chains A

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

Pockets

12 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Interfaces

6 interfaces between chains.

• A–B · 951 Ų buried · 10 hydrogen bonds · protein-protein
• C–D · 913 Ų buried · 9 hydrogen bonds · protein-protein
• A–D · 529 Ų buried · 7 hydrogen bonds · protein-protein
• B–C · 527 Ų buried · 3 hydrogen bonds · protein-protein
• A–C · 428 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

• 6HK2 · Crystal structure of ferric R-state human methemoglobin bound to maleimide-deferoxamine… · 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 6HK2 · PDBe 6HK2 · UniProt P69905 · UniProt P68871