2hhe Summary

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OXYGEN AFFINITY MODULATION BY THE N-TERMINI OF THE BETA CHAINS IN HUMAN AND BOVINE HEMOGLOBIN

The structure was published by Fronticelli, C., Pechik, I., Brinigar, W.S., Kowalczyk, J., and Gilliland, G.L., in 1994 in a paper entitled "Chloride ion independence of the Bohr effect in a mutant human hemoglobin beta (V1M+H2deleted)." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 1994.

The experimental data on which the structure is based was not deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely HEMOGLOBIN (DEOXY) (ALPHA CHAIN) and HEMOGLOBIN (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 (DEOXY) (ALPHA CHAIN) P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
C HEMOGLOBIN (DEOXY) (ALPHA CHAIN) P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
B HEMOGLOBIN (DEOXY) (BETA CHAIN) P68871 (4-147) (HBB_HUMAN)search Homo sapienssearch 98% 145 100%
D HEMOGLOBIN (DEOXY) (BETA CHAIN) P68871 (4-147) (HBB_HUMAN)search Homo sapienssearch 98% 145 100%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P69905 (2 - 142) HEMOGLOBIN (DEOXY) (ALPHA CHAIN) Homo sapiens
P68871 (4 - 147) HEMOGLOBIN (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 Biological process (GO) Molecular function (GO) Cellular component (GO)
A, C (P69905) oxygen transportsearch hydrogen peroxide catabolic processsearch oxidation-reduction processsearch response to hydrogen peroxidesearch protein heterooligomerizationsearch positive regulation of cell deathsearch small molecule metabolic processsearch bicarbonate transportsearch transportsearch iron ion bindingsearch heme bindingsearch oxygen bindingsearch protein bindingsearch haptoglobin bindingsearch peroxidase activitysearch metal ion bindingsearch oxygen transporter activitysearch haptoglobin-hemoglobin complexsearch extracellular regionsearch extracellular vesicular exosomesearch cytosolsearch hemoglobin complexsearch blood microparticlesearch membranesearch endocytic vesicle lumensearch cytosolic small ribosomal subunitsearch
B, D (P68871) regulation of blood vessel sizesearch positive regulation of cell deathsearch nitric oxide transportsearch response to hydrogen peroxidesearch regulation of blood pressuresearch bicarbonate transportsearch oxygen transportsearch platelet aggregationsearch hydrogen peroxide catabolic processsearch positive regulation of nitric oxide biosynthetic processsearch protein heterooligomerizationsearch renal absorptionsearch transportsearch small molecule metabolic processsearch oxidation-reduction processsearch blood coagulationsearch heme bindingsearch oxygen bindingsearch protein bindingsearch metal ion bindingsearch oxygen transporter activitysearch hemoglobin bindingsearch peroxidase activitysearch iron ion bindingsearch haptoglobin bindingsearch cytosolsearch hemoglobin complexsearch extracellular regionsearch extracellular vesicular exosomesearch endocytic vesicle lumensearch haptoglobin-hemoglobin complexsearch blood microparticlesearch

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