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