1o1m Summary

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Deoxy hemoglobin (A-GLYGLYGLY-C:V1M,L29F,H58Q B,D:V1M,V67W)

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