Ligand migration and cavities within scapharca dimeric hemoglobin: wild type with co bound to heme and chloropropyl benzene bound to the XE4 cavity

Structure

x-ray diffraction · 1 distinct chain · 81% helix, 0% strand (DSSP).

Ligands and binding sites

• HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
• LT1 · (3-chloropropyl)benzene · ligand · chains A
• CMO · Carbon monoxide · ion · 2 copies · chains A, B

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 957 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

• 3G53 · Ligand migration and cavities within scapharca dimeric hemoglobin: wild type with co… · the same entry in another collection · chain A against A, TM-score 1.00
• P02213 · AlphaFold monomer V2.0 prediction for globin-1 (P02213) · a predicted model of the same protein · 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 P02213
• Elsewhere: RCSB PDB 3G53 · PDBe 3G53 · UniProt P02213