3kmf Summary


Room Temperature Time-of-Flight Neutron Diffraction Study of Deoxy Human Normal Adult Hemoglobin

The structure was published by Kovalevsky, A.Y., Chatake, T., Shibayama, N., et al., Fisher, Z., Langan, P., and Morimoto, Y., in 2010 in a paper entitled "Direct Determination of Protonation States of Histidine Residues in a 2 A Neutron Structure of Deoxy-Human Normal Adult Hemoglobin and Implications for the Bohr Effect." (abstract).

The structure was determined using Neutron diffraction at a resolution of 2.0 Å and deposited in 2009.

The experimental data on which the structure is based was also deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely Hemoglobin subunit alpha and Hemoglobin subunit beta.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms heterotetramers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Hemoglobin subunit alpha P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
E Hemoglobin subunit alpha P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
C Hemoglobin subunit beta P68871 (2-147) (HBB_HUMAN)search Homo sapienssearch 98% 146 100%
G Hemoglobin subunit beta P68871 (2-147) (HBB_HUMAN)search Homo sapienssearch 98% 146 100%

This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P69905 (2 - 142) Hemoglobin subunit alpha Homo sapiens
P68871 (2 - 147) Hemoglobin subunit beta Homo sapiens

Chain Structural classification (CATH) Sequence family (Pfam)
A, E (P69905) Globinssearch PF00042: Globinsearch
C, G (P68871) Globinssearch PF00042: Globinsearch

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
A, E (P69905) heme bindingsearch protein bindingsearch oxygen bindingsearch metal ion bindingsearch oxygen transporter activitysearch haptoglobin bindingsearch peroxidase activitysearch iron ion bindingsearch hemoglobin complexsearch extracellular vesicular exosomesearch endocytic vesicle lumensearch extracellular regionsearch haptoglobin-hemoglobin complexsearch membranesearch cytosolsearch cytosolic small ribosomal subunitsearch blood microparticlesearch bicarbonate transportsearch oxygen transportsearch transportsearch hydrogen peroxide catabolic processsearch positive regulation of cell deathsearch oxidation-reduction processsearch response to hydrogen peroxidesearch small molecule metabolic processsearch protein heterooligomerizationsearch
C, G (P68871) protein bindingsearch peroxidase activitysearch oxygen transporter activitysearch heme bindingsearch oxygen bindingsearch metal ion bindingsearch hemoglobin bindingsearch haptoglobin bindingsearch iron ion bindingsearch hemoglobin complexsearch cytosolsearch extracellular regionsearch extracellular vesicular exosomesearch blood microparticlesearch haptoglobin-hemoglobin complexsearch endocytic vesicle lumensearch response to hydrogen peroxidesearch positive regulation of cell deathsearch platelet aggregationsearch protein heterooligomerizationsearch regulation of blood pressuresearch oxygen transportsearch blood coagulationsearch positive regulation of nitric oxide biosynthetic processsearch regulation of blood vessel sizesearch small molecule metabolic processsearch hydrogen peroxide catabolic processsearch transportsearch bicarbonate transportsearch nitric oxide transportsearch oxidation-reduction processsearch renal absorptionsearch

Chain InterPro annotation
A, E Globinsearch Haemoglobin, alphasearch Haemoglobin, pisearch Globin-likesearch Globin, structural domainsearch
C, G Globinsearch Haemoglobin, betasearch Globin-likesearch Globin, structural domainsearch