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

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