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) Not available
Homo sapienssearch Not available 146 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P69905 (2 - 142) HEMOGLOBIN (CARBONMONOXY) (ALPHA 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 oxygen bindingsearch protein bindingsearch peroxidase activitysearch haptoglobin bindingsearch oxygen transporter activitysearch metal ion bindingsearch iron ion bindingsearch extracellular regionsearch endocytic vesicle lumensearch cytosolsearch extracellular vesicular exosomesearch haptoglobin-hemoglobin complexsearch hemoglobin complexsearch cytosolic small ribosomal subunitsearch blood microparticlesearch membranesearch protein heterooligomerizationsearch oxygen transportsearch hydrogen peroxide catabolic processsearch transportsearch bicarbonate transportsearch oxidation-reduction processsearch positive regulation of cell deathsearch small molecule metabolic processsearch response to hydrogen peroxidesearch
B () oxygen bindingsearch heme bindingsearch oxygen transporter activitysearch peroxidase activitysearch protein bindingsearch hemoglobin bindingsearch metal ion bindingsearch iron ion bindingsearch haptoglobin bindingsearch endocytic vesicle lumensearch extracellular regionsearch cytosolsearch hemoglobin complexsearch extracellular vesicular exosomesearch haptoglobin-hemoglobin complexsearch blood microparticlesearch oxygen transportsearch blood coagulationsearch bicarbonate transportsearch response to hydrogen peroxidesearch renal absorptionsearch transportsearch hydrogen peroxide catabolic processsearch protein heterooligomerizationsearch regulation of blood pressuresearch positive regulation of cell deathsearch platelet aggregationsearch small molecule metabolic processsearch regulation of blood vessel sizesearch nitric oxide transportsearch oxidation-reduction processsearch positive regulation of nitric oxide biosynthetic processsearch

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