1gli Summary



The structure was published by Vallone, B., Bellelli, A., Miele, A.E., Brunori, M., and Fermi, G., in 1996 in a paper entitled "Probing the alpha 1 beta 2 interface of human hemoglobin by mutagenesis. Role of the FG-C contact regions." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.5 Å and deposited in 1996.

The experimental data on which the structure is based was also deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely DEOXYHEMOGLOBIN.

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 DEOXYHEMOGLOBIN P69905 (3-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
C DEOXYHEMOGLOBIN P69905 (3-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
B DEOXYHEMOGLOBIN P68871 (3-147) (HBB_HUMAN)search Homo sapienssearch 98% 146 100%
D DEOXYHEMOGLOBIN P68871 (3-147) (HBB_HUMAN)search Homo sapienssearch 98% 146 100%

This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P69905 (3 - 142) DEOXYHEMOGLOBIN Homo sapiens
P68871 (3 - 147) DEOXYHEMOGLOBIN 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) iron ion bindingsearch oxygen bindingsearch heme bindingsearch protein bindingsearch metal ion bindingsearch oxygen transporter activitysearch peroxidase activitysearch haptoglobin bindingsearch oxygen transportsearch bicarbonate transportsearch hydrogen peroxide catabolic processsearch small molecule metabolic processsearch positive regulation of cell deathsearch response to hydrogen peroxidesearch protein heterooligomerizationsearch oxidation-reduction processsearch receptor-mediated endocytosissearch transportsearch extracellular regionsearch extracellular exosomesearch membranesearch cytosolic small ribosomal subunitsearch endocytic vesicle lumensearch cytosolsearch haptoglobin-hemoglobin complexsearch hemoglobin complexsearch blood microparticlesearch
B, D (P68871) heme bindingsearch oxygen transporter activitysearch oxygen bindingsearch haptoglobin bindingsearch protein bindingsearch hemoglobin bindingsearch metal ion bindingsearch peroxidase activitysearch iron ion bindingsearch oxygen transportsearch small molecule metabolic processsearch hydrogen peroxide catabolic processsearch blood coagulationsearch bicarbonate transportsearch positive regulation of cell deathsearch regulation of blood vessel sizesearch transportsearch positive regulation of nitric oxide biosynthetic processsearch oxidation-reduction processsearch receptor-mediated endocytosissearch protein heterooligomerizationsearch renal absorptionsearch nitric oxide transportsearch regulation of blood pressuresearch response to hydrogen peroxidesearch platelet aggregationsearch hemoglobin complexsearch cytosolsearch extracellular exosomesearch haptoglobin-hemoglobin complexsearch extracellular regionsearch blood microparticlesearch 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