1dke Summary

pdbe.org/1dke
spacer

NI BETA HEME HUMAN HEMOGLOBIN

The structure was published by Bruno, S., Bettati, S., Manfredini, M., et al., Tsuneshige, A., Yonetani, T., and Henry, E.R., in 2000 in a paper entitled "Oxygen binding by alpha(Fe2+)2beta(Ni2+)2 hemoglobin crystals." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 1999.

The experimental data on which the structure is based was not deposited.

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

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