1bij Summary

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CROSSLINKED, DEOXY HUMAN HEMOGLOBIN A

The structure was published by Fernandez, E.J., Abad-Zapatero, C., and Olsen, K.W., in 2000 in a paper entitled "Crystal structure of Lysbeta(1)82-Lysbeta(2)82 crosslinked hemoglobin: a possible allosteric intermediate" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.3 Å and deposited in 1998.

The experimental data on which the structure is based was not deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely HEMOGLOBIN A.

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 A P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
C HEMOGLOBIN A P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
B HEMOGLOBIN A P68871 (2-147) (HBB_HUMAN)search Homo sapienssearch 98% 146 100%
D HEMOGLOBIN A 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 A Homo sapiens
P68871 (2 - 147) HEMOGLOBIN A 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 heme bindingsearch haptoglobin bindingsearch oxygen bindingsearch oxygen transporter activitysearch metal ion bindingsearch hemoglobin complexsearch extracellular regionsearch extracellular vesicular exosomesearch cytosolsearch haptoglobin-hemoglobin complexsearch cytosolic small ribosomal subunitsearch blood microparticlesearch membranesearch endocytic vesicle lumensearch oxygen transportsearch positive regulation of cell deathsearch receptor-mediated endocytosissearch protein heterooligomerizationsearch oxidation-reduction processsearch response to hydrogen peroxidesearch bicarbonate transportsearch transportsearch small molecule metabolic processsearch hydrogen peroxide catabolic processsearch
B, D (P68871) oxygen bindingsearch protein bindingsearch haptoglobin bindingsearch iron ion bindingsearch heme bindingsearch oxygen transporter activitysearch peroxidase activitysearch metal ion bindingsearch hemoglobin bindingsearch cytosolsearch endocytic vesicle lumensearch extracellular vesicular exosomesearch extracellular regionsearch hemoglobin complexsearch blood microparticlesearch haptoglobin-hemoglobin complexsearch oxygen transportsearch regulation of blood pressuresearch small molecule metabolic processsearch receptor-mediated endocytosissearch regulation of blood vessel sizesearch hydrogen peroxide catabolic processsearch protein heterooligomerizationsearch transportsearch blood coagulationsearch bicarbonate transportsearch positive regulation of nitric oxide biosynthetic processsearch positive regulation of cell deathsearch renal absorptionsearch response to hydrogen peroxidesearch nitric oxide transportsearch platelet aggregationsearch oxidation-reduction 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