1o1m Summary

pdbe.org/1o1m
spacer

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