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