1qi8 Summary

pdbe.org/1qi8
spacer

DEOXYGENATED STRUCTURE OF A DISTAL POCKET HEMOGLOBIN MUTANT

The structure was published by Miele, A.E., Santanche, S., Travaglini-Allocatelli, C., Vallone, B., Brunori, M., and Bellelli, A., in 1999 in a paper entitled "Modulation of ligand binding in engineered human hemoglobin distal pocket." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 1999.

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 (3-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
C HEMOGLOBIN P69905 (3-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
B HEMOGLOBIN P68871 (3-147) (HBB_HUMAN)search Homo sapienssearch 98% 146 100%
D HEMOGLOBIN P68871 (3-147) (HBB_HUMAN)search Homo sapienssearch 98% 146 100%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P69905 (3 - 142) HEMOGLOBIN Homo sapiens
P68871 (3 - 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 Biological process (GO) Cellular component (GO) Molecular function (GO)
A, C (P69905) oxygen transportsearch small molecule metabolic processsearch receptor-mediated endocytosissearch hydrogen peroxide catabolic processsearch bicarbonate transportsearch response to hydrogen peroxidesearch protein heterooligomerizationsearch positive regulation of cell deathsearch transportsearch oxidation-reduction processsearch hemoglobin complexsearch blood microparticlesearch endocytic vesicle lumensearch extracellular regionsearch haptoglobin-hemoglobin complexsearch extracellular exosomesearch cytosolsearch cytosolic small ribosomal subunitsearch membranesearch iron ion bindingsearch oxygen bindingsearch heme bindingsearch protein bindingsearch metal ion bindingsearch peroxidase activitysearch haptoglobin bindingsearch oxygen transporter activitysearch
B, D (P68871) bicarbonate transportsearch oxygen transportsearch renal absorptionsearch blood coagulationsearch positive regulation of nitric oxide biosynthetic processsearch hydrogen peroxide catabolic processsearch receptor-mediated endocytosissearch protein heterooligomerizationsearch response to hydrogen peroxidesearch positive regulation of cell deathsearch small molecule metabolic processsearch nitric oxide transportsearch platelet aggregationsearch oxidation-reduction processsearch regulation of blood vessel sizesearch regulation of blood pressuresearch transportsearch hemoglobin complexsearch blood microparticlesearch extracellular exosomesearch endocytic vesicle lumensearch extracellular regionsearch cytosolsearch haptoglobin-hemoglobin complexsearch iron ion bindingsearch heme bindingsearch oxygen bindingsearch protein bindingsearch peroxidase activitysearch hemoglobin bindingsearch oxygen transporter activitysearch haptoglobin bindingsearch metal ion bindingsearch

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