1o1p Summary

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Deoxy hemoglobin (A-GLY-C:V1M; B,D:V1M,C93A,N108K)

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% 283 100%
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 (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 protein bindingsearch metal ion bindingsearch haptoglobin bindingsearch heme bindingsearch peroxidase activitysearch oxygen transporter activitysearch oxygen bindingsearch positive regulation of cell deathsearch response to hydrogen peroxidesearch oxygen transportsearch hydrogen peroxide catabolic processsearch oxidation-reduction processsearch bicarbonate transportsearch protein heterooligomerizationsearch transportsearch small molecule metabolic processsearch hemoglobin complexsearch cytosolsearch endocytic vesicle lumensearch haptoglobin-hemoglobin complexsearch extracellular regionsearch extracellular vesicular exosomesearch membranesearch cytosolic small ribosomal subunitsearch blood microparticlesearch
B, D (P68871) peroxidase activitysearch haptoglobin bindingsearch heme bindingsearch protein bindingsearch oxygen bindingsearch oxygen transporter activitysearch hemoglobin bindingsearch metal ion bindingsearch iron ion bindingsearch renal absorptionsearch bicarbonate transportsearch oxygen transportsearch positive regulation of nitric oxide biosynthetic processsearch nitric oxide transportsearch response to hydrogen peroxidesearch regulation of blood pressuresearch platelet aggregationsearch transportsearch blood coagulationsearch regulation of blood vessel sizesearch positive regulation of cell deathsearch hydrogen peroxide catabolic processsearch small molecule metabolic processsearch oxidation-reduction processsearch protein heterooligomerizationsearch extracellular regionsearch endocytic vesicle lumensearch hemoglobin complexsearch cytosolsearch haptoglobin-hemoglobin complexsearch blood microparticlesearch extracellular vesicular exosomesearch

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