2DN1: Hemoglobin alpha subunit

1.25A resolution crystal structure of human hemoglobin in the oxy form. Determined by X-ray diffraction at 1.25 Å resolution. Released 9 May 2006.

Method
X-ray diffraction
Resolution
1.25 Å
Organism
Homo sapiens
Chains
2
Atoms
2,506
Mol. weight
32.52 kDa
Ligands
MBN, OXY, HEM
Released
9 May 2006

Explore 2DN1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2DN1 contains 24 α-helices and 0 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 11 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix4-1714
α-helix18-203
α-helix21-3515
α-helix37-426
α-helix53-7119
α-helix73-753
α-helix76-794
α-helix81-855
α-helix86-905
α-helix95-11218
α-helix119-13618
Chain B: 13 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix5-1511
α-helix23-3412
α-helix36-416
α-helix43-453
α-helix51-566
α-helix58-7518
α-helix81-844
α-helix86-894
α-helix90-956
α-helix101-11818
α-helix119-1213
α-helix124-14118
α-helix143-1453

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Hemoglobin alpha subunitAprotein141Homo sapiensP69905 (AlphaFold model)
Hemoglobin beta subunitBprotein146Homo sapiensP68871 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2DN1_1 Hemoglobin alpha subunit (chains A)
VLSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFDLSHGSAQVKGHGK
KVADALTNAVAHVDDMPNALSALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPA
VHASLDKFLASVSTVLTSKYR
Sequence of entity 2 (B), FASTA
>2DN1_2 Hemoglobin beta subunit (chains B)
VHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKV
KAHGKKVLGAFSDGLAHLDNLKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGK
EFTPPVQAAYQKVVAGVANALAHKYH

Ligands and cofactors

IDNameFormulaCopies
MBNTolueneC7 H82
OXYOxygen moleculeO22
HEMProtoporphyrin IX containing FEC34 H32 Fe N4 O42

Primary citation

1.25 a resolution crystal structures of human haemoglobin in the oxy, deoxy and carbonmonoxy forms. Park, S.-Y., Yokoyama, T., Shibayama, N. et al. J Mol Biol (2006) 360:690-701. DOI 10.1016/j.jmb.2006.05.036 · PubMed

Other PDB entries of the same protein (UniProt P69905 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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