1o1l Summary

pdbe.org/1o1l
spacer

Deoxy hemoglobin (A-GLY-C:V1M,L29W,H58Q; 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% 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 oxygen bindingsearch heme bindingsearch metal ion bindingsearch protein bindingsearch peroxidase activitysearch haptoglobin bindingsearch oxygen transporter activitysearch oxygen transportsearch small molecule metabolic processsearch hydrogen peroxide catabolic processsearch bicarbonate transportsearch protein heterooligomerizationsearch positive regulation of cell deathsearch response to hydrogen peroxidesearch oxidation-reduction processsearch receptor-mediated endocytosissearch transportsearch extracellular exosomesearch membranesearch hemoglobin complexsearch extracellular regionsearch endocytic vesicle lumensearch cytosolic small ribosomal subunitsearch haptoglobin-hemoglobin complexsearch cytosolsearch blood microparticlesearch
B, D (P68871) iron ion bindingsearch heme bindingsearch oxygen bindingsearch protein bindingsearch peroxidase activitysearch metal ion bindingsearch oxygen transporter activitysearch hemoglobin bindingsearch haptoglobin bindingsearch oxygen transportsearch positive regulation of nitric oxide biosynthetic processsearch bicarbonate transportsearch receptor-mediated endocytosissearch protein heterooligomerizationsearch blood coagulationsearch renal absorptionsearch positive regulation of cell deathsearch oxidation-reduction processsearch small molecule metabolic processsearch hydrogen peroxide catabolic processsearch regulation of blood vessel sizesearch response to hydrogen peroxidesearch regulation of blood pressuresearch platelet aggregationsearch transportsearch nitric oxide transportsearch hemoglobin complexsearch haptoglobin-hemoglobin complexsearch extracellular exosomesearch extracellular regionsearch cytosolsearch endocytic vesicle lumensearch blood microparticlesearch

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