1gbu Summary

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DEOXY (BETA-(C93A,C112G)) HUMAN HEMOGLOBIN

The structure was published by Vasquez, G.B., Karavitis, M., Ji, X., et al., Brinigar, W.S., Gilliland, G.L., and Fronticelli, C., in 1999 in a paper entitled "Cysteines beta93 and beta112 as probes of conformational and functional events at the human hemoglobin subunit interfaces." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 1996.

The experimental data on which the structure is based was not deposited.

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

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 P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
C HEMOGLOBIN P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
B HEMOGLOBIN P68871 (2-147) (HBB_HUMAN)search Homo sapienssearch 98% 146 100%
D HEMOGLOBIN 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 Homo sapiens
P68871 (2 - 147) HEMOGLOBIN 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 haptoglobin bindingsearch peroxidase activitysearch oxygen transportsearch bicarbonate transportsearch oxidation-reduction processsearch protein heterooligomerizationsearch hydrogen peroxide catabolic processsearch small molecule metabolic processsearch receptor-mediated endocytosissearch positive regulation of cell deathsearch response to hydrogen peroxidesearch transportsearch hemoglobin complexsearch cytosolsearch extracellular exosomesearch extracellular regionsearch membranesearch blood microparticlesearch haptoglobin-hemoglobin complexsearch endocytic vesicle lumensearch cytosolic small ribosomal subunitsearch
B, D (P68871) iron ion bindingsearch oxygen bindingsearch protein bindingsearch oxygen transporter activitysearch haptoglobin bindingsearch hemoglobin bindingsearch metal ion bindingsearch peroxidase activitysearch heme bindingsearch small molecule metabolic processsearch hydrogen peroxide catabolic processsearch oxygen transportsearch renal absorptionsearch bicarbonate transportsearch positive regulation of nitric oxide biosynthetic processsearch platelet aggregationsearch protein heterooligomerizationsearch transportsearch receptor-mediated endocytosissearch response to hydrogen peroxidesearch blood coagulationsearch nitric oxide transportsearch oxidation-reduction processsearch regulation of blood vessel sizesearch regulation of blood pressuresearch positive regulation of cell deathsearch hemoglobin complexsearch haptoglobin-hemoglobin complexsearch cytosolsearch extracellular regionsearch extracellular exosomesearch endocytic vesicle lumensearch blood microparticlesearch

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