1thb Summary

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REFINEMENT OF A PARTIALLY OXYGENATED T STATE HAEMOGLOBIN AT 1.5 ANGSTROMS RESOLUTION

The structure was published by Waller, D.A. and Liddington, R.C., in 1990 in a paper entitled "Refinement of a partially oxygenated T state human haemoglobin at 1.5 A resolution." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.5 Å and deposited in 1990.

The experimental data on which the structure is based was also deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely HEMOGLOBIN A (OXY) (ALPHA CHAIN) and HEMOGLOBIN A (DEOXY) (BETA CHAIN).

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 A (OXY) (ALPHA CHAIN) P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
C HEMOGLOBIN A (OXY) (ALPHA CHAIN) P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
B HEMOGLOBIN A (DEOXY) (BETA CHAIN) P68871 (2-147) (HBB_HUMAN)search Homo sapienssearch 98% 146 100%
D HEMOGLOBIN A (DEOXY) (BETA CHAIN) 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 A (OXY) (ALPHA CHAIN) Homo sapiens
P68871 (2 - 147) HEMOGLOBIN A (DEOXY) (BETA CHAIN) 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) iron ion bindingsearch protein bindingsearch heme bindingsearch peroxidase activitysearch metal ion bindingsearch oxygen bindingsearch haptoglobin bindingsearch oxygen transporter activitysearch hydrogen peroxide catabolic processsearch oxygen transportsearch oxidation-reduction processsearch bicarbonate transportsearch protein heterooligomerizationsearch response to hydrogen peroxidesearch small molecule metabolic processsearch positive regulation of cell deathsearch transportsearch extracellular vesicular exosomesearch hemoglobin complexsearch cytosolsearch endocytic vesicle lumensearch extracellular regionsearch cytosolic small ribosomal subunitsearch membranesearch blood microparticlesearch haptoglobin-hemoglobin complexsearch
B, D (P68871) oxygen bindingsearch protein bindingsearch peroxidase activitysearch haptoglobin bindingsearch hemoglobin bindingsearch iron ion bindingsearch heme bindingsearch oxygen transporter activitysearch metal ion bindingsearch oxygen transportsearch bicarbonate transportsearch oxidation-reduction processsearch small molecule metabolic processsearch positive regulation of nitric oxide biosynthetic processsearch hydrogen peroxide catabolic processsearch response to hydrogen peroxidesearch regulation of blood pressuresearch blood coagulationsearch renal absorptionsearch transportsearch nitric oxide transportsearch platelet aggregationsearch protein heterooligomerizationsearch positive regulation of cell deathsearch regulation of blood vessel sizesearch extracellular regionsearch endocytic vesicle lumensearch blood microparticlesearch hemoglobin complexsearch cytosolsearch extracellular vesicular exosomesearch 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