1o1o Summary

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Deoxy hemoglobin (A,C:V1M,V62L; B,D:V1M,V67L)

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

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