› 1uiw

X-ray diffraction
1.5Å resolution

Crystal Structures of Unliganded and Half-Liganded Human Hemoglobin Derivatives Cross-Linked between Lys 82beta1 and Lys 82beta2

Released:
DOI: 10.2210/pdb1uiw/pdb
PDB entry 1uiw coloured by chain, front view.
PDB entry 1uiw coloured by chain, side view.
PDB entry 1uiw coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of unliganded and half-liganded human hemoglobin derivatives cross-linked between Lys 82beta1 and Lys 82beta2.
Park SY, Shibayama N, Hiraki T, Tame JR
Biochemistry 43 8711-7 (2004)
PMID: 15236579

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 Chains: A, C, E, G
Molecule details ›
Chains: A, C, E, G
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
Molecule details ›
Chains: B, D, F, H
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 8 x HEM
Ligand 2FU 2 x 2FU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44B2
Spacegroup: P21
Unit cell:
a: 66.137Å b: 96.338Å c: 102.476Å
α: 90° β: 101.79° γ: 90°
R-values:
R R work R free
0.173 0.172 0.205

Quick links

Citations

5 citation in other articles

1.25 A resolution crystal structures of human haemoglobin in the oxy, deoxy and carbonmonoxy forms.
Park et al. (2006)
4 more

1 mention without citation

Properties of Cavities in Biological Structures-A Survey of the Protein Data Bank.
Chwastyk et al. (2020)