1gzx Summary

pdbe.org/1gzx
spacer

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

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