2DXM

Neutron Structure Analysis of Deoxy Human Hemoglobin

Summary for 2DXM

• Entry DOI: 10.2210/pdb2dxm/pdb
• Descriptor: Hemoglobin subunit alpha, Hemoglobin subunit beta, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
• Functional Keywords: alpha2-beta2, oxygen storage-transport complex, oxygen storage/transport
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 4
• Total formula weight: 64547.05

Authors

Morimoto, Y. (deposition date: 2006-08-28, release date: 2007-12-04, Last modification date: 2024-04-03)

Primary citation

Chatake, T.,Shibayama, N.,Park, S.Y.,Kurihara, K.,Tamada, T.,Tanaka, I.,Niimura, N.,Kuroki, R.,Morimoto, Y.
Protonation states of buried histidine residues in human deoxyhemoglobin revealed by neutron crystallography.
J.Am.Chem.Soc., 129:14840-14841, 2007

PubMed Abstract: The protonation states of buried histidine residues in human deoxyhemoglobin were unambiguously identified by using a neutron crystallographic technique. Unexpectedly, the neutron structure reveals that both the alpha- and beta-distal histidines (Hisalpha58 and Hisbeta63) adopt a positively charged, fully (doubly) protonated form, suggesting their contribution to the Bohr effect. In addition, the neutron data provide an accurate picture of the alpha1beta1 hydrogen-bonding network and allow us to observe unambiguously the nature of the intradimeric interactions at an atomic level.

PubMed: 17990881
DOI: 10.1021/ja0749441

Experimental method

NEUTRON DIFFRACTION (2.1 Å)