1dke Summary

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