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

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