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) Not available
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 Cellular component (GO) Molecular function (GO) Biological process (GO)
A, C (P69905) extracellular regionsearch cytosolsearch extracellular vesicular exosomesearch haptoglobin-hemoglobin complexsearch blood microparticlesearch membranesearch cytosolic small ribosomal subunitsearch hemoglobin complexsearch endocytic vesicle lumensearch protein bindingsearch oxygen bindingsearch heme bindingsearch haptoglobin bindingsearch peroxidase activitysearch oxygen transporter activitysearch iron ion bindingsearch metal ion bindingsearch hydrogen peroxide catabolic processsearch protein heterooligomerizationsearch response to hydrogen peroxidesearch positive regulation of cell deathsearch oxygen transportsearch small molecule metabolic processsearch oxidation-reduction processsearch bicarbonate transportsearch transportsearch
B, D (P68871) extracellular regionsearch hemoglobin complexsearch extracellular vesicular exosomesearch endocytic vesicle lumensearch cytosolsearch blood microparticlesearch haptoglobin-hemoglobin complexsearch oxygen bindingsearch protein bindingsearch oxygen transporter activitysearch hemoglobin bindingsearch metal ion bindingsearch peroxidase activitysearch haptoglobin bindingsearch heme bindingsearch iron ion bindingsearch oxidation-reduction processsearch oxygen transportsearch regulation of blood pressuresearch positive regulation of cell deathsearch bicarbonate transportsearch positive regulation of nitric oxide biosynthetic processsearch protein heterooligomerizationsearch response to hydrogen peroxidesearch nitric oxide transportsearch hydrogen peroxide catabolic processsearch renal absorptionsearch platelet aggregationsearch regulation of blood vessel sizesearch blood coagulationsearch small molecule metabolic processsearch transportsearch

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