2dn3 Summary

pdbe.org/2dn3
spacer

1.25A resolution crystal structure of human hemoglobin in the carbonmonoxy form

The structure was published by Park, S.-Y., Yokoyama, T., Shibayama, N., Shiro, Y., and Tame, J.R., in 2006 in a paper entitled "1.25 a resolution crystal structures of human haemoglobin in the oxy, deoxy and carbonmonoxy forms." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.25 Å and deposited in 2006.

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

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

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 alpha subunit P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
B Hemoglobin beta subunit 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 alpha subunit Homo sapiens
P68871 (2 - 147) Hemoglobin beta subunit Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P69905) Globinssearch Globinssearch PF00042: Globinsearch
B (P68871) Globinssearch Globinssearch PF00042: Globinsearch

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

Chain InterPro annotation
A Globinsearch Haemoglobin, alphasearch Haemoglobin, pisearch Globin-likesearch Globin, structural domainsearch
B Globinsearch Haemoglobin, betasearch Globin-likesearch Globin, structural domainsearch