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