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

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