› 1k1k

X-ray diffraction
2Å resolution

Structure of Mutant Human Carbonmonoxyhemoglobin C (beta E6K) at 2.0 Angstrom Resolution in Phosphate Buffer.

Released:
DOI: 10.2210/pdb1k1k/pdb
PDB entry 1k1k coloured by chain, front view.
PDB entry 1k1k coloured by chain, side view.
PDB entry 1k1k coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of mutant human carbonmonoxyhemoglobin C (betaE6K) at 2.0 A resolution.
Dewan JC, Feeling-Taylor A, Puius YA, Patskovska L, Patskovsky Y, Nagel RL, Almo SC, Hirsch RE
Acta Crystallogr D Biol Crystallogr 58 2038-42 (2002)
PMID: 12454462

Function and Biology Details

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

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 Chain: A
Molecule details ›
Chain: A
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
Structure domains: Globins
Hemoglobin subunit beta Chain: B
Molecule details ›
Chain: B
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
Structure domains: Globins

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P41212
Unit cell:
a: 54.16Å b: 54.16Å c: 195.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.183 0.238

Quick links

Citations

2 citation in other articles

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

4 mentions without citation

Identification of phosphorylated proteins in erythrocytes infected by the human malaria parasite Plasmodium falciparum.
Wu et al. (2009)
3 more