1m9p Summary

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Crystalline Human Carbonmonoxy Hemoglobin C Exhibits The R2 Quaternary State at Neutral pH In The Presence of Polyethylene Glycol: The 2.1 Angstrom Resolution Crystal Structure

The structure was published by Patskovska, L.N., Patskovsky, Y.V., Almo, S.C., and Hirsch, R.E., in 2005 in a paper entitled "COHbC and COHbS crystallize in the R2 quaternary state at neutral pH in the presence of PEG 4000." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 2002.

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