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The structure of human carbonmonoxy haemoglobin at 2.7 ångströms resolution

Analyse The structure of human carbonmonoxy haemoglobin at 2.7 ångströms resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1HCO
Type
protein
Length
287 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hemoglobin (carbonmonoxy) (alpha chain); Hemoglobin (carbonmonoxy) (beta chain)
UniProt
P69905, P68871
Ligands
HEM, CMO
Pockets
3 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 64% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHemoglobin (carbonmonoxy) (alpha chain)protein14169% helix, 0% strandP69905
BHemoglobin (carbonmonoxy) (beta chain)protein14660% helix, 0% strandP68871

Ligands and binding sites

  • HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
  • 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

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12560.750.8829HEM, CMO
22080.710.8624HEM, CMO
32420.550.7734empty

Interfaces

1 interface between chains.

  • A–B · 943 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 1HCO · The structure of human carbonmonoxy haemoglobin at 2.7 ångströms resolution · the same entry in another collection · chain A against A, TM-score 1.00

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