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

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