1rqa Summary

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Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin. Beta W73E hemoglobin exposed to NO under anaerobic conditions

The structure was published by Chan, N.-L., Kavanaugh, J.S., Rogers, P.H., and Arnone, A., in 2004 in a paper entitled "Crystallographic analysis of the interaction of nitric oxide with quaternary-T human hemoglobin." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.11 Å and deposited in 2003.

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%
C 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%
D 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, C (P69905) Globinssearch Globinssearch PF00042: Globinsearch
B, D (P68871) Globinssearch Globinssearch PF00042: Globinsearch

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

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