1rps Summary

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

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