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