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

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