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 Biological process (GO) Molecular function (GO) Cellular component (GO)
A, C (P69905) small molecule metabolic processsearch oxygen transportsearch positive regulation of cell deathsearch oxidation-reduction processsearch bicarbonate transportsearch hydrogen peroxide catabolic processsearch transportsearch protein heterooligomerizationsearch response to hydrogen peroxidesearch haptoglobin bindingsearch protein bindingsearch oxygen transporter activitysearch heme bindingsearch iron ion bindingsearch metal ion bindingsearch oxygen bindingsearch peroxidase activitysearch extracellular regionsearch extracellular vesicular exosomesearch haptoglobin-hemoglobin complexsearch cytosolsearch hemoglobin complexsearch endocytic vesicle lumensearch membranesearch blood microparticlesearch cytosolic small ribosomal subunitsearch
B, D (P68871) oxygen transportsearch hydrogen peroxide catabolic processsearch bicarbonate transportsearch small molecule metabolic processsearch oxidation-reduction processsearch platelet aggregationsearch transportsearch positive regulation of nitric oxide biosynthetic processsearch nitric oxide transportsearch regulation of blood pressuresearch protein heterooligomerizationsearch renal absorptionsearch regulation of blood vessel sizesearch positive regulation of cell deathsearch response to hydrogen peroxidesearch blood coagulationsearch hemoglobin bindingsearch protein bindingsearch haptoglobin bindingsearch oxygen bindingsearch metal ion bindingsearch oxygen transporter activitysearch iron ion bindingsearch peroxidase activitysearch heme bindingsearch extracellular vesicular exosomesearch extracellular regionsearch 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