1vwt Summary

pdbe.org/1vwt
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T STATE HUMAN HEMOGLOBIN [ALPHA V96W], ALPHA AQUOMET, BETA DEOXY

The structure was published by Puius, Y.A., Zou, M., Ho, N.T., Ho, C., and Almo, S.C., in 1998 in a paper entitled "Novel water-mediated hydrogen bonds as the structural basis for the low oxygen affinity of the blood substitute candidate rHb(alpha 96Val-->Trp)." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.9 Å and deposited in 1997.

The experimental data on which the structure is based was not deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely HEMOGLOBIN.

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 P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
C HEMOGLOBIN P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
B HEMOGLOBIN P68871 (2-147) (HBB_HUMAN)search Homo sapienssearch 98% 146 100%
D HEMOGLOBIN P68871 (2-147) (HBB_HUMAN)search Homo sapienssearch 98% 146 100%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P69905 (2 - 142) HEMOGLOBIN Homo sapiens
P68871 (2 - 147) HEMOGLOBIN 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) heme bindingsearch oxygen bindingsearch iron ion bindingsearch protein bindingsearch oxygen transporter activitysearch haptoglobin bindingsearch metal ion bindingsearch peroxidase activitysearch oxygen transportsearch oxidation-reduction processsearch receptor-mediated endocytosissearch bicarbonate transportsearch protein heterooligomerizationsearch hydrogen peroxide catabolic processsearch positive regulation of cell deathsearch small molecule metabolic processsearch response to hydrogen peroxidesearch transportsearch cytosolsearch hemoglobin complexsearch extracellular regionsearch extracellular vesicular exosomesearch cytosolic small ribosomal subunitsearch endocytic vesicle lumensearch membranesearch haptoglobin-hemoglobin complexsearch blood microparticlesearch
B, D (P68871) iron ion bindingsearch oxygen bindingsearch heme bindingsearch protein bindingsearch oxygen transporter activitysearch peroxidase activitysearch hemoglobin bindingsearch metal ion bindingsearch haptoglobin bindingsearch oxygen transportsearch positive regulation of nitric oxide biosynthetic processsearch positive regulation of cell deathsearch nitric oxide transportsearch protein heterooligomerizationsearch regulation of blood pressuresearch bicarbonate transportsearch hydrogen peroxide catabolic processsearch transportsearch response to hydrogen peroxidesearch small molecule metabolic processsearch regulation of blood vessel sizesearch platelet aggregationsearch renal absorptionsearch receptor-mediated endocytosissearch blood coagulationsearch oxidation-reduction processsearch hemoglobin complexsearch endocytic vesicle lumensearch extracellular vesicular exosomesearch blood microparticlesearch extracellular regionsearch haptoglobin-hemoglobin complexsearch cytosolsearch

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