2d5z Summary

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Crystal structure of T-state human hemoglobin complexed with three 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 1.45 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 Biological process (GO) Molecular function (GO) Cellular component (GO)
A, C (P69905) oxygen transportsearch transportsearch positive regulation of cell deathsearch bicarbonate transportsearch protein heterooligomerizationsearch oxidation-reduction processsearch small molecule metabolic processsearch response to hydrogen peroxidesearch hydrogen peroxide catabolic processsearch peroxidase activitysearch protein bindingsearch oxygen bindingsearch iron ion bindingsearch heme bindingsearch metal ion bindingsearch haptoglobin bindingsearch oxygen transporter activitysearch hemoglobin complexsearch extracellular vesicular exosomesearch haptoglobin-hemoglobin complexsearch extracellular regionsearch cytosolic small ribosomal subunitsearch endocytic vesicle lumensearch membranesearch blood microparticlesearch cytosolsearch
B, D (P68871) oxygen transportsearch regulation of blood vessel sizesearch response to hydrogen peroxidesearch protein heterooligomerizationsearch nitric oxide transportsearch small molecule metabolic processsearch positive regulation of cell deathsearch renal absorptionsearch hydrogen peroxide catabolic processsearch regulation of blood pressuresearch transportsearch bicarbonate transportsearch positive regulation of nitric oxide biosynthetic processsearch platelet aggregationsearch oxidation-reduction processsearch blood coagulationsearch protein bindingsearch metal ion bindingsearch oxygen bindingsearch iron ion bindingsearch heme bindingsearch hemoglobin bindingsearch oxygen transporter activitysearch peroxidase activitysearch haptoglobin bindingsearch extracellular regionsearch hemoglobin complexsearch endocytic vesicle lumensearch cytosolsearch haptoglobin-hemoglobin complexsearch extracellular vesicular exosomesearch blood microparticlesearch

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