2dn3 Summary

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