› 6kau

X-ray diffraction
1.6Å resolution

Carbonmonoxy human hemoglobin A in the R2 quaternary structure at 140 K: Dark

Released:
DOI: 10.2210/pdb6kau/pdb
PDB entry 6kau coloured by chain, front view.
PDB entry 6kau coloured by chain, side view.
PDB entry 6kau coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Direct observation of ligand migration within human hemoglobin at work.
Shibayama N, Sato-Tomita A, Ohki M, Ichiyanagi K, Park SY
Proc Natl Acad Sci U S A 117 4741-4748 (2020)
PMID: 32071219

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159519 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Hemoglobin subunit alpha Chains: A, C
Molecule details ›
Chains: A, C
Length: 141 amino acids
Theoretical weight: 15.15 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P69905 (Residues: 2-142; Coverage: 99%)
Gene names: HBA1, HBA2
Sequence domains: Globin
Hemoglobin subunit beta Chains: B, D
Molecule details ›
Chains: B, D
Length: 146 amino acids
Theoretical weight: 15.89 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P68871 (Residues: 2-147; Coverage: 99%)
Gene name: HBB
Sequence domains: Globin

Ligands and Environments

2 bound ligands:
Ligand HEM 4 x HEM
Ligand CMO 4 x CMO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P212121
Unit cell:
a: 61.124Å b: 96.436Å c: 100.263Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.178 0.213

Quick links

Citations

1 review citation

Kinetic mechanisms for O2 binding to myoglobins and hemoglobins.
Olson JS. (2022)
5 other articles

1 mention without citation

Direct observation of ligand migration within human hemoglobin at work.
Shibayama et al. (2020)