1kd2 Summary

pdbe.org/1kd2
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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 small molecule metabolic processsearch hydrogen peroxide catabolic processsearch protein heterooligomerizationsearch bicarbonate transportsearch transportsearch receptor-mediated endocytosissearch positive regulation of cell deathsearch oxidation-reduction processsearch response to hydrogen peroxidesearch iron ion bindingsearch oxygen bindingsearch heme bindingsearch oxygen transporter activitysearch haptoglobin bindingsearch protein bindingsearch metal ion bindingsearch peroxidase activitysearch hemoglobin complexsearch extracellular vesicular exosomesearch cytosolsearch membranesearch extracellular regionsearch haptoglobin-hemoglobin complexsearch cytosolic small ribosomal subunitsearch endocytic vesicle lumensearch blood microparticlesearch
B, D (P68871) renal absorptionsearch bicarbonate transportsearch protein heterooligomerizationsearch oxygen transportsearch nitric oxide transportsearch hydrogen peroxide catabolic processsearch regulation of blood pressuresearch blood coagulationsearch positive regulation of nitric oxide biosynthetic processsearch transportsearch platelet aggregationsearch small molecule metabolic processsearch oxidation-reduction processsearch receptor-mediated endocytosissearch positive regulation of cell deathsearch regulation of blood vessel sizesearch response to hydrogen peroxidesearch iron ion bindingsearch oxygen bindingsearch heme bindingsearch protein bindingsearch oxygen transporter activitysearch haptoglobin bindingsearch metal ion bindingsearch hemoglobin bindingsearch peroxidase activitysearch extracellular regionsearch extracellular vesicular exosomesearch endocytic vesicle lumensearch haptoglobin-hemoglobin complexsearch cytosolsearch hemoglobin complexsearch 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