6hbw Summary

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Crystal structure of deoxy-human hemoglobin beta6 glu->trp

The structure was published by Harrington, D.J., Adachi, K., and Royer Jr., W.E., in 1998 in a paper entitled "Crystal structure of deoxy-human hemoglobin beta6 Glu --> Trp. Implications for the structure and formation of the sickle cell fiber." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 1998.

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

This PDB entry contains a complex of 2 biomacromolecules, namely PROTEIN (HEMOGLOBIN ALPHA 1) and PROTEIN (HEMOGLOBIN BETA).

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 PROTEIN (HEMOGLOBIN ALPHA 1) P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
C PROTEIN (HEMOGLOBIN ALPHA 1) P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
B PROTEIN (HEMOGLOBIN BETA) P68871 (2-147) (HBB_HUMAN)search Homo sapienssearch 98% 146 100%
D PROTEIN (HEMOGLOBIN BETA) 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) PROTEIN (HEMOGLOBIN ALPHA 1) Homo sapiens
P68871 (2 - 147) PROTEIN (HEMOGLOBIN BETA) 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) heme bindingsearch iron ion bindingsearch oxygen bindingsearch protein bindingsearch haptoglobin bindingsearch peroxidase activitysearch oxygen transporter activitysearch metal ion bindingsearch hemoglobin complexsearch extracellular regionsearch endocytic vesicle lumensearch blood microparticlesearch extracellular vesicular exosomesearch haptoglobin-hemoglobin complexsearch cytosolsearch membranesearch cytosolic small ribosomal subunitsearch oxygen transportsearch protein heterooligomerizationsearch hydrogen peroxide catabolic processsearch bicarbonate transportsearch small molecule metabolic processsearch oxidation-reduction processsearch transportsearch response to hydrogen peroxidesearch positive regulation of cell deathsearch
B, D (P68871) oxygen bindingsearch iron ion bindingsearch heme bindingsearch haptoglobin bindingsearch oxygen transporter activitysearch protein bindingsearch hemoglobin bindingsearch metal ion bindingsearch peroxidase activitysearch hemoglobin complexsearch extracellular regionsearch extracellular vesicular exosomesearch blood microparticlesearch haptoglobin-hemoglobin complexsearch cytosolsearch endocytic vesicle lumensearch oxygen transportsearch bicarbonate transportsearch nitric oxide transportsearch regulation of blood pressuresearch renal absorptionsearch positive regulation of cell deathsearch blood coagulationsearch positive regulation of nitric oxide biosynthetic processsearch response to hydrogen peroxidesearch oxidation-reduction processsearch transportsearch protein heterooligomerizationsearch platelet aggregationsearch small molecule metabolic processsearch regulation of blood vessel sizesearch hydrogen peroxide catabolic 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