1mko Summary

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A Fourth Quaternary Structure of Human Hemoglobin A at 2.18 A Resolution

The structure was published by Safo, M.K. and Abraham, D.J., in 2005 in a paper entitled "The enigma of the liganded hemoglobin end state: a novel quaternary structure of human carbonmonoxy hemoglobin." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.18 Å and deposited in 2002.

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