1o1n Summary

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Deoxy hemoglobin (A-GLYGLYGLY-C:V1M,L29W; B,D:V1M)

The structure has not been published. The depositing authors are Brucker, E.A.search

This crystal structure was determined using X-ray diffraction at a resolution of 1.8 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 heterotrimers.

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% 285 98%
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 (P69905) Globinssearch Globinssearch PF00042: Globinsearch
B, D (P68871) Globinssearch Globinssearch PF00042: Globinsearch

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

Chain InterPro annotation
A Globinsearch Haemoglobin, alphasearch Haemoglobin, pisearch Globin-likesearch Globin, structural domainsearch
B, D Globinsearch Haemoglobin, betasearch Globin-likesearch Globin, structural domainsearch