1gbv Summary

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(ALPHA-OXY, BETA-(C112G)DEOXY) T-STATE 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 2.0 Å and deposited in 1995.

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