1rq3 Summary

pdbe.org/1rq3
spacer

Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Deoxyhemoglobin, Deoxyhemoglobin

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

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