1gli Summary

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DEOXYHEMOGLOBIN T38W (ALPHA CHAINS), V1G (ALPHA AND BETA CHAINS)

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) Cellular component (GO) Biological process (GO)
A, C (P69905) iron ion bindingsearch protein bindingsearch oxygen bindingsearch metal ion bindingsearch peroxidase activitysearch oxygen transporter activitysearch haptoglobin bindingsearch heme bindingsearch hemoglobin complexsearch extracellular regionsearch extracellular vesicular exosomesearch cytosolic small ribosomal subunitsearch membranesearch endocytic vesicle lumensearch haptoglobin-hemoglobin complexsearch cytosolsearch blood microparticlesearch bicarbonate transportsearch small molecule metabolic processsearch hydrogen peroxide catabolic processsearch positive regulation of cell deathsearch oxidation-reduction processsearch oxygen transportsearch transportsearch response to hydrogen peroxidesearch protein heterooligomerizationsearch
B, D (P68871) heme bindingsearch protein bindingsearch oxygen transporter activitysearch oxygen bindingsearch haptoglobin bindingsearch hemoglobin bindingsearch metal ion bindingsearch iron ion bindingsearch peroxidase activitysearch extracellular vesicular exosomesearch cytosolsearch hemoglobin complexsearch haptoglobin-hemoglobin complexsearch extracellular regionsearch blood microparticlesearch endocytic vesicle lumensearch small molecule metabolic processsearch bicarbonate transportsearch positive regulation of cell deathsearch regulation of blood pressuresearch hydrogen peroxide catabolic processsearch regulation of blood vessel sizesearch oxidation-reduction processsearch oxygen transportsearch positive regulation of nitric oxide biosynthetic processsearch transportsearch renal absorptionsearch protein heterooligomerizationsearch response to hydrogen peroxidesearch blood coagulationsearch platelet aggregationsearch nitric oxide transportsearch

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