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

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