1rq4 Summary

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Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin, HEMOGLOBIN EXPOSED TO NO UNDER AEROBIC 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) Biological process (GO) Cellular component (GO)
A, C (P69905) heme bindingsearch iron ion bindingsearch oxygen bindingsearch protein bindingsearch metal ion bindingsearch oxygen transporter activitysearch haptoglobin bindingsearch peroxidase activitysearch oxygen transportsearch small molecule metabolic processsearch hydrogen peroxide catabolic processsearch bicarbonate transportsearch protein heterooligomerizationsearch oxidation-reduction processsearch transportsearch positive regulation of cell deathsearch response to hydrogen peroxidesearch hemoglobin complexsearch cytosolsearch extracellular vesicular exosomesearch extracellular regionsearch blood microparticlesearch membranesearch endocytic vesicle lumensearch cytosolic small ribosomal subunitsearch haptoglobin-hemoglobin complexsearch
B, D (P68871) iron ion bindingsearch heme bindingsearch oxygen bindingsearch protein bindingsearch peroxidase activitysearch oxygen transporter activitysearch hemoglobin bindingsearch metal ion bindingsearch haptoglobin bindingsearch oxygen transportsearch positive regulation of nitric oxide biosynthetic processsearch response to hydrogen peroxidesearch transportsearch renal absorptionsearch nitric oxide transportsearch oxidation-reduction processsearch regulation of blood vessel sizesearch protein heterooligomerizationsearch bicarbonate transportsearch blood coagulationsearch regulation of blood pressuresearch small molecule metabolic processsearch positive regulation of cell deathsearch hydrogen peroxide catabolic processsearch hemoglobin complexsearch extracellular regionsearch endocytic vesicle lumensearch extracellular vesicular exosomesearch cytosolsearch blood microparticlesearch haptoglobin-hemoglobin complexsearch

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