1kd2 Summary

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Crystal Structure of Human Deoxyhemoglobin in Absence of Any Anions

A publication describing this structure is not available. The depositing authors are Colombo, M.F.search; Seixas, F.A.V.search

This crystal structure was determined using X-ray diffraction at a resolution of 1.87 Å and deposited in 2001.

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

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

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 chain P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
C Hemoglobin alpha chain P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
B Hemoglobin beta chain P68871 (2-147) (HBB_HUMAN)search Homo sapienssearch 98% 146 100%
D Hemoglobin beta chain 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 chain Homo sapiens
P68871 (2 - 147) Hemoglobin beta chain Homo sapiens

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

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

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