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

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