2d60 Summary

pdbe.org/2d60
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Crystal structure of deoxy human hemoglobin complexed with two L35 molecules

The structure was published by Yokoyama, T., Neya, S., Tsuneshige, A., Yonetani, T., Park, S.Y., and Tame, J.R., in 2006 in a paper entitled "R-state haemoglobin with low oxygen affinity: crystal structures of deoxy human and carbonmonoxy horse haemoglobin bound to the effector molecule L35" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.7 Å and deposited in 2005.

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

This PDB entry contains a complex of 2 biomacromolecules, namely Hemoglobin alpha subunit and Hemoglobin beta subunit.

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 subunit P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
C Hemoglobin alpha subunit P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
B Hemoglobin beta subunit P68871 (2-147) (HBB_HUMAN)search Homo sapienssearch 98% 146 99%
D Hemoglobin beta subunit P68871 (2-147) (HBB_HUMAN)search Homo sapienssearch 98% 146 99%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P69905 (2 - 142) Hemoglobin alpha subunit Homo sapiens
P68871 (2 - 147) Hemoglobin beta subunit 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 metal ion bindingsearch protein bindingsearch heme bindingsearch peroxidase activitysearch haptoglobin bindingsearch oxygen transporter activitysearch iron ion bindingsearch extracellular vesicular exosomesearch extracellular regionsearch membranesearch cytosolsearch blood microparticlesearch hemoglobin complexsearch haptoglobin-hemoglobin complexsearch endocytic vesicle lumensearch cytosolic small ribosomal subunitsearch transportsearch small molecule metabolic processsearch response to hydrogen peroxidesearch bicarbonate transportsearch oxygen transportsearch positive regulation of cell deathsearch hydrogen peroxide catabolic processsearch protein heterooligomerizationsearch oxidation-reduction processsearch
B, D (P68871) oxygen bindingsearch protein bindingsearch hemoglobin bindingsearch haptoglobin bindingsearch peroxidase activitysearch metal ion bindingsearch iron ion bindingsearch oxygen transporter activitysearch heme bindingsearch blood microparticlesearch extracellular vesicular exosomesearch extracellular regionsearch hemoglobin complexsearch endocytic vesicle lumensearch cytosolsearch haptoglobin-hemoglobin complexsearch oxidation-reduction processsearch blood coagulationsearch oxygen transportsearch hydrogen peroxide catabolic processsearch bicarbonate transportsearch regulation of blood pressuresearch positive regulation of nitric oxide biosynthetic processsearch renal absorptionsearch transportsearch positive regulation of cell deathsearch small molecule metabolic processsearch nitric oxide transportsearch regulation of blood vessel sizesearch response to hydrogen peroxidesearch protein heterooligomerizationsearch platelet aggregationsearch

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