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