Crystal structure of carbonmonoxy hemoglobin S (liganded sickle cell hemoglobin) complexed with GBT440, co-crystallization experiment

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
• 5L7 · 2-methyl-3-({2-[1-(propan-2-yl)-1H-pyrazol-5-yl]pyridin-3-yl}methoxy)phenol · ligand · chains A, C
• UNL · Unknown ligand · ligand · chains B, C
• CMO · Carbon monoxide · ion · 4 copies · chains A, B, C, D
• GOL · Glycerol · additive · 3 copies · chains A, D

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

Pockets

8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Interfaces

6 interfaces between chains.

• C–D · 910 Ų buried · 12 hydrogen bonds · protein-protein
• A–B · 906 Ų buried · 10 hydrogen bonds · protein-protein
• B–C · 453 Ų buried · 3 hydrogen bonds · protein-protein
• A–D · 448 Ų buried · 4 hydrogen bonds · protein-protein
• A–C · 383 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

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

Compared structures

• 5E83 · Crystal structure of carbonmonoxy hemoglobin S (liganded sickle cell hemoglobin)… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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• Every structure of UniProt P69905
• Every structure of UniProt P68871
• Elsewhere: RCSB PDB 5E83 · PDBe 5E83 · UniProt P69905 · UniProt P68871