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

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