4h2l

X-ray diffraction
1.78Å resolution

Deer mouse hemoglobin in hydrated format

Released:
Source organism: Peromyscus maniculatus
Primary publication:
Deer mouse hemoglobin exhibits a lowered oxygen affinity owing to mobility of the E helix.
Acta Crystallogr Sect F Struct Biol Cryst Commun 69 393-8 (2013)
PMID: 23545644

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-107529 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Globin domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 141 amino acids
Theoretical weight: 14.94 KDa
Source organism: Peromyscus maniculatus
Expression system: Escherichia coli
UniProt:
  • Canonical: A4ZQ95 (Residues: 2-142; Coverage: 99%)
Gene names: HBA, Hba
Sequence domains: Globin
Structure domains: Globins
Globin domain-containing protein Chain: B
Molecule details ›
Chain: B
Length: 146 amino acids
Theoretical weight: 15.86 KDa
Source organism: Peromyscus maniculatus
Expression system: Escherichia coli
UniProt:
  • Canonical: C5MQT7 (Residues: 2-147; Coverage: 99%)
Gene names: HBB, HBB-T1, HBB-T2
Sequence domains: Globin
Structure domains: Globins

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: C2221
Unit cell:
a: 76.675Å b: 80.061Å c: 86.848Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.162 0.201
Expression system: Escherichia coli