1gbv Summary

pdbe.org/1gbv
spacer

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

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