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