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

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