1a0z 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 2.0 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) protein bindingsearch peroxidase activitysearch iron ion bindingsearch heme bindingsearch oxygen bindingsearch metal ion bindingsearch haptoglobin bindingsearch oxygen transporter activitysearch transportsearch protein heterooligomerizationsearch bicarbonate transportsearch positive regulation of cell deathsearch hydrogen peroxide catabolic processsearch oxygen transportsearch receptor-mediated endocytosissearch response to hydrogen peroxidesearch small molecule metabolic processsearch oxidation-reduction processsearch endocytic vesicle lumensearch extracellular vesicular exosomesearch extracellular regionsearch cytosolsearch membranesearch blood microparticlesearch hemoglobin complexsearch haptoglobin-hemoglobin complexsearch cytosolic small ribosomal subunitsearch
B, D (P68871) protein bindingsearch hemoglobin bindingsearch heme bindingsearch oxygen transporter activitysearch peroxidase activitysearch oxygen bindingsearch iron ion bindingsearch haptoglobin bindingsearch metal ion bindingsearch renal absorptionsearch platelet aggregationsearch blood coagulationsearch bicarbonate transportsearch transportsearch regulation of blood vessel sizesearch oxygen transportsearch small molecule metabolic processsearch response to hydrogen peroxidesearch receptor-mediated endocytosissearch positive regulation of nitric oxide biosynthetic processsearch regulation of blood pressuresearch protein heterooligomerizationsearch oxidation-reduction processsearch positive regulation of cell deathsearch nitric oxide transportsearch hydrogen peroxide catabolic processsearch blood microparticlesearch endocytic vesicle lumensearch extracellular vesicular exosomesearch extracellular regionsearch cytosolsearch hemoglobin complexsearch 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