PDBsum entry 3qw4

Transferase, lyase

PDB id: 3qw4

Contents

Protein chains

445 a.a.

Ligands

U5P ×3

Metals

_CL

Waters ×41

PDB id:

3qw4

Name:

Transferase, lyase

Title:

Structure of leishmania donovani ump synthase

Structure:

Ump synthase. Chain: b, c. Fragment: unp residues 1-452. Engineered: yes

Source:

Leishmania donovani. Organism_taxid: 5661. Gene: ldbpk_160560. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

3.00Å R-factor: 0.239 R-free: 0.304

Authors:

J.B.French,S.E.Ealick

Key ref:

J.B.French et al. (2011). The Leishmania donovani UMP synthase is essential for promastigote viability and has an unusual tetrameric structure that exhibits substrate-controlled oligomerization. J Biol Chem, 286, 20930-20941. PubMed id: 21507942

Date:

26-Feb-11 Release date: 20-Apr-11

Protein chains

H9ABT8  (H9ABT8_LEIDO) -  Orotidine 5'-phosphate decarboxylase from Leishmania donovani

Seq: 457 a.a.

Struc: 445 a.a.

Enzyme reactions

• Enzyme class: E.C.4.1.1.23 - orotidine-5'-phosphate decarboxylase.
• Pathway: Pyrimidine Biosynthesis
• Reaction: orotidine 5'-phosphate + H⁺ = UMP + CO2

orotidine 5'-phosphate + H(+) = UMP + CO2 (Bound ligand (Het Group name = U5P) corresponds exactly)

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

reference

J Biol Chem 286:20930-20941 (2011)

PubMed id: 21507942

The Leishmania donovani UMP synthase is essential for promastigote viability and has an unusual tetrameric structure that exhibits substrate-controlled oligomerization.

J.B.French, P.A.Yates, D.R.Soysa, J.M.Boitz, N.S.Carter, B.Chang, B.Ullman, S.E.Ealick.

ABSTRACT

No abstract given.