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

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