2dn1 Summary

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PDB entry 2dn1 (supersedes 2dfo)

1.25A resolution crystal structure of human hemoglobin in the oxy 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 99%
B Hemoglobin beta subunit P68871 (2-147) (HBB_HUMAN)search Homo sapienssearch 98% 146 99%


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