PDBsum entry 2pc5

Hydrolase

PDB id

2pc5

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Contents

			Protein chains

					127 a.a. *

			Metals

					_MG

			Waters ×212

* Residue conservation analysis

PDB id:

2pc5

Links
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Name:

Hydrolase

Title:

Native crystal structure analysis on arabidopsis dutpase

Structure:

Dutp pyrophosphatase-like protein. Chain: a, b, c. Engineered: yes

Source:

Arabidopsis thaliana. Thale cress. Organism_taxid: 3702. Gene: t6h20.30. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

Resolution:

2.20Å

R-factor:

0.185

R-free:

0.251

Authors:

H.Moriyama,M.Bajaj

Key ref:

M.Bajaj and H.Moriyama (2007). Purification, crystallization and preliminary crystallographic analysis of deoxyuridine triphosphate nucleotidohydrolase from Arabidopsis thaliana. Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 409-411. PubMed id: 17565183

Date:

29-Mar-07

Release date:

12-Feb-08

PROCHECK

	Headers

	References

Protein chains

Q9STG6 (DUT_ARATH) - Deoxyuridine 5'-triphosphate nucleotidohydrolase from Arabidopsis thaliana

Seq: Struc:					166 a.a. 127 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.3.6.1.23 - dUTP diphosphatase.

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

Reaction:

dUTP + H2O = dUMP + diphosphate + H⁺

dUTP	+	H2O	=	dUMP	+	diphosphate	+	H(+)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

	Acta Crystallogr Sect F Struct Biol Cryst Commun 63:409-411 (2007)
PubMed id: 17565183

Purification, crystallization and preliminary crystallographic analysis of deoxyuridine triphosphate nucleotidohydrolase from Arabidopsis thaliana.
M.Bajaj, H.Moriyama.

ABSTRACT

The deoxyuridine triphosphate nucleotidohydrolase gene from Arabidopsis thaliana was expressed and the gene product was purified. Crystallization was performed by the hanging-drop vapour-diffusion method at 298 K using 2 M ammonium sulfate as the precipitant. X-ray diffraction data were collected to 2.2 A resolution using Cu K alpha radiation. The crystal belongs to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 69.90, b = 70.86 A, c = 75.55 A. Assuming the presence of a trimer in the asymmetric unit, the solvent content was 30%, with a V(M) of 1.8 A3 Da(-1).

Literature references that cite this PDB file's key reference

PubMed id

Reference

19851015

K.Homma, and H.Moriyama (2009).
Crystallization and crystal-packing studies of Chlorella virus deoxyuridine triphosphatase.

Acta Crystallogr Sect F Struct Biol Cryst Commun, 65, 1030-1034.

PDB codes:

3c2t 3c3i 3ca9

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