1fn3 Summary

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CRYSTAL STRUCTURE OF NICKEL RECONSTITUTED HEMOGLOBIN-A CASE FOR PERMANENT, T-STATE HEMOGLOBIN

The structure was published by Venkateshrao, S., Deepthi, S., Pattabhi, V., and Manoharan, P.T., in 2003 in a paper entitled "Crystal Structure of Nickel Reconstituted Hemoglobin - A Case for Permanent, T-State Hemoglobin" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.48 Å and deposited in 2000.

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

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