PDBsum entry 1thb

Oxygen transport

PDB id

1thb

Loading ...

Contents

			Protein chains

					141 a.a. *


					146 a.a. *

			Ligands

					HEM-OXY ×2


					HEM ×2


					IHP

			Waters ×314

* Residue conservation analysis

PDB id:

1thb

Links

Name:

Oxygen transport

Title:

Refinement of a partially oxygenated t state haemoglobin at 1.5 angstroms resolution

Structure:

Hemoglobin a (oxy) (alpha chain). Chain: a, c. Engineered: yes. Hemoglobin a (deoxy) (beta chain). Chain: b, d. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Organism_taxid: 9606

Biol. unit:

Tetramer (from PQS)

Resolution:

1.50Å

R-factor:

0.196

Authors:

D.A.Waller,R.C.Liddington

Key ref:

D.A.Waller and R.C.Liddington (1990). Refinement of a partially oxygenated T state human haemoglobin at 1.5 A resolution. Acta Crystallogr B, 46, 409-418. PubMed id: 2383372

Date:

23-Jan-90

Release date:

15-Jan-91

PROCHECK

	Headers

	References

Protein chains

P69905 (HBA_HUMAN) - Hemoglobin subunit alpha from Homo sapiens

Seq: Struc:					142 a.a. 141 a.a.

Protein chains

P68871 (HBB_HUMAN) - Hemoglobin subunit beta from Homo sapiens

Seq: Struc:					147 a.a. 146 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

Chains A, B, C, D: E.C.?

[IntEnz] [ExPASy] [KEGG] [BRENDA]

	Acta Crystallogr B 46:409-418 (1990)
PubMed id: 2383372

Refinement of a partially oxygenated T state human haemoglobin at 1.5 A resolution.
D.A.Waller, R.C.Liddington.

ABSTRACT

The degree of ligation of T state human haemoglobin crystals is reduced by inositol hexaphosphate (IHP). The structure of a partially ligated haemoglobin has been refined using fast Fourier restrained-least-squares techniques. Manual interventions were required to escape from local minima and introduce a large number of solvent molecules. Individual isotropic temperature factors were refined for all atoms and the final average atomic temperature factor is 32.3 A2. The final R factor is 19.6% for all data between 10 and 1.5 A. The final model consists of 4560 protein atoms and 313 solvent molecules. The occupancies of the ligand atoms and the anisotropic behaviour of the iron atoms have been refined, demonstrating that the alpha haem groups are only partially ligated and that there is no ligation of the beta haems. Density for the IHP indicates that it is not well ordered even though changes in the ligation and structure of the haemoglobin indicate its presence.

Literature references that cite this PDB file's key reference

PubMed id

Reference

12023247

L.Mouawad, D.Perahia, C.H.Robert, and C.Guilbert (2002).
New insights into the allosteric mechanism of human hemoglobin from molecular dynamics simulations.

Biophys J, 82, 3224-3245.

11566768

A.Riccio, M.Tamburrini, B.Giardina, and G.di Prisco (2001).
Molecular dynamics analysis of a second phosphate site in the hemoglobins of the seabird, south polar skua. Is there a site-site migratory mechanism along the central cavity?

Biophys J, 81, 1938-1946.

9041656

A.Mozzarelli, C.Rivetti, G.L.Rossi, W.A.Eaton, and E.R.Henry (1997).
Allosteric effectors do not alter the oxygen affinity of hemoglobin crystals.

Protein Sci, 6, 484-489.

8563637

R.M.Stroud, and E.B.Fauman (1995).
Significance of structural changes in proteins: expected errors in refined protein structures.

Protein Sci, 4, 2392-2404.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.