2hco Summary

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THE STRUCTURE OF HUMAN CARBONMONOXY HAEMOGLOBIN AT 2.7 ANGSTROMS RESOLUTION

The structure was published by Baldwin, J.M., in 1980 in a paper entitled "The structure of human carbonmonoxy haemoglobin at 2.7 A resolution." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.7 Å and deposited in 1979.

The experimental data on which the structure is based was not deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely HEMOGLOBIN (CARBONMONOXY) (ALPHA CHAIN) and HEMOGLOBIN (CARBONMONOXY) (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 (CARBONMONOXY) (ALPHA CHAIN) P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
B HEMOGLOBIN (CARBONMONOXY) (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 (CARBONMONOXY) (ALPHA CHAIN) Homo sapiens
P68871 (2 - 147) HEMOGLOBIN (CARBONMONOXY) (BETA CHAIN) 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) oxygen bindingsearch heme bindingsearch iron ion bindingsearch protein bindingsearch peroxidase activitysearch haptoglobin bindingsearch metal ion bindingsearch oxygen transporter activitysearch protein heterooligomerizationsearch oxygen transportsearch oxidation-reduction processsearch hydrogen peroxide catabolic processsearch receptor-mediated endocytosissearch transportsearch positive regulation of cell deathsearch response to hydrogen peroxidesearch bicarbonate transportsearch small molecule metabolic processsearch endocytic vesicle lumensearch hemoglobin complexsearch extracellular regionsearch cytosolsearch extracellular vesicular exosomesearch cytosolic small ribosomal subunitsearch blood microparticlesearch membranesearch haptoglobin-hemoglobin complexsearch
B (P68871) heme bindingsearch iron ion bindingsearch protein bindingsearch oxygen transporter activitysearch oxygen bindingsearch peroxidase activitysearch hemoglobin bindingsearch haptoglobin bindingsearch metal ion bindingsearch oxygen transportsearch renal absorptionsearch response to hydrogen peroxidesearch bicarbonate transportsearch blood coagulationsearch positive regulation of cell deathsearch regulation of blood pressuresearch hydrogen peroxide catabolic processsearch protein heterooligomerizationsearch small molecule metabolic processsearch oxidation-reduction processsearch transportsearch positive regulation of nitric oxide biosynthetic processsearch receptor-mediated endocytosissearch platelet aggregationsearch regulation of blood vessel sizesearch nitric oxide transportsearch extracellular regionsearch endocytic vesicle lumensearch cytosolsearch hemoglobin complexsearch extracellular vesicular exosomesearch blood microparticlesearch haptoglobin-hemoglobin complexsearch

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