1aj9 Summary

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R-STATE HUMAN CARBONMONOXYHEMOGLOBIN ALPHA-A53S

The structure was published by Vasquez, G.B., Ji, X., Fronticelli, C., and Gilliland, G.L., in 1998 in a paper entitled "Human carboxyhemoglobin at 2.2 A resolution: structure and solvent comparisons of R-state, R2-state and T-state hemoglobins." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 1997.

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

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