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

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