› 4n7n

X-ray diffraction
2.75Å resolution

Capturing the haemoglobin allosteric transition in a single crystal form; Crystal structure of full-liganded human haemoglobin with phosphate at 2.75 A resolution.

Released:
DOI: 10.2210/pdb4n7n/pdb
PDB entry 4n7n coloured by chain, front view.
PDB entry 4n7n coloured by chain, side view.
PDB entry 4n7n coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Capturing the hemoglobin allosteric transition in a single crystal form.
Shibayama N, Sugiyama K, Tame JR, Park SY
J Am Chem Soc 136 5097-105 (2014)
PMID: 24635037

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, E, G, I, K
Molecule details ›
Chains: A, C, E, G, I, K
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 Chains: B, D, F, H, J, L
Molecule details ›
Chains: B, D, F, H, J, L
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

1 bound ligand:
Ligand HEM 12 x HEM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: C2
Unit cell:
a: 227.619Å b: 56.061Å c: 141.555Å
α: 90° β: 102.49° γ: 90°
R-values:
R R work R free
0.251 0.251 0.286

Quick links

Citations

1 review citation

From protein structure to function via single crystal optical spectroscopy.
Ronda et al. (2015)
14 other articles

5 mentions without citation

New look at hemoglobin allostery.
Yuan et al. (2015)
4 more