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