1qi8 Summary

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