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

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