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