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