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

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