1gzx Summary

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OXY T STATE HAEMOGLOBIN: OXYGEN BOUND AT ALL FOUR HAEMS

The structure was published by Paoli, M., Liddington, R., Tame, J., Wilkinson, A., and Dodson, G., in 1996 in a paper entitled "Crystal Structure of T State Haemoglobin with Oxygen Bound at All Four Haems." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 2002.

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

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