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

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