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