1j7y Summary

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Crystal structure of partially ligated mutant of HbA

The structure was published by Miele, A.E., Draghi, F., Arcovito, A., et al., Brunori, M., Travaglini-Allocatelli, C., and Vallone, B., in 2001 in a paper entitled "Control of heme reactivity by diffusion: structural basis and functional characterization in hemoglobin mutants." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.7 Å and deposited in 2001.

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

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

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