1a0u Summary

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HEMOGLOBIN (VAL BETA1 MET) MUTANT

The structure was published by Kavanaugh, J.S., Weydert, J.A., Rogers, P.H., and Arnone, A., in 1998 in a paper entitled "High-resolution crystal structures of human hemoglobin with mutations at tryptophan 37beta: structural basis for a high-affinity T-state,." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.14 Å and deposited in 1997.

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 (3-147) (HBB_HUMAN)search Homo sapienssearch 98% 146 100%
D HEMOGLOBIN (BETA CHAIN) P68871 (3-147) (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 (3 - 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) Biological process (GO) Cellular component (GO)
A, C (P69905) heme bindingsearch oxygen bindingsearch protein bindingsearch peroxidase activitysearch haptoglobin bindingsearch metal ion bindingsearch oxygen transporter activitysearch iron ion bindingsearch oxidation-reduction processsearch receptor-mediated endocytosissearch positive regulation of cell deathsearch bicarbonate transportsearch small molecule metabolic processsearch oxygen transportsearch hydrogen peroxide catabolic processsearch protein heterooligomerizationsearch transportsearch response to hydrogen peroxidesearch extracellular regionsearch extracellular exosomesearch hemoglobin complexsearch membranesearch endocytic vesicle lumensearch haptoglobin-hemoglobin complexsearch cytosolsearch blood microparticlesearch cytosolic small ribosomal subunitsearch
B, D (P68871) iron ion bindingsearch heme bindingsearch oxygen bindingsearch haptoglobin bindingsearch oxygen transporter activitysearch protein bindingsearch hemoglobin bindingsearch metal ion bindingsearch peroxidase activitysearch oxygen transportsearch regulation of blood vessel sizesearch small molecule metabolic processsearch bicarbonate transportsearch platelet aggregationsearch hydrogen peroxide catabolic processsearch protein heterooligomerizationsearch receptor-mediated endocytosissearch blood coagulationsearch positive regulation of nitric oxide biosynthetic processsearch oxidation-reduction processsearch regulation of blood pressuresearch positive regulation of cell deathsearch nitric oxide transportsearch renal absorptionsearch response to hydrogen peroxidesearch transportsearch extracellular regionsearch extracellular exosomesearch hemoglobin complexsearch cytosolsearch haptoglobin-hemoglobin complexsearch 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