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