PDBsum entry 3nqd

Lyase/lyase inhibitor

PDB id: 3nqd

Contents

Protein chains

219 a.a.

Ligands

BMP ×2

GOL

Waters ×393

PDB id:

3nqd

Name:

Lyase/lyase inhibitor

Title:

Crystal structure of the mutant i96t of orotidine 5'-monophosphate decarboxylase from methanobacterium thermoautotrophicum complexed with inhibitor bmp

Structure:

Orotidine 5'-phosphate decarboxylase. Chain: a, b. Synonym: omp decarboxylase, ompdcase, ompdecase. Engineered: yes. Mutation: yes

Source:

Methanothermobacter thermautotrophicus. Organism_taxid: 145262. Gene: pyrf, mth_129. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.42Å R-factor: 0.166 R-free: 0.185

Authors:

A.A.Fedorov,E.V.Fedorov,B.M.Wood,J.A.Gerlt,S.C.Almo

Key ref:

V.Iiams et al. (2011). Mechanism of the orotidine 5'-monophosphate decarboxylase-catalyzed reaction: importance of residues in the orotate binding site. Biochemistry, 50, 8497-8507. PubMed id: 21870810

Date:

29-Jun-10 Release date: 11-May-11

Protein chains

O26232  (PYRF_METTH) -  Orotidine 5'-phosphate decarboxylase from Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)

Seq: 228 a.a.

Struc: 219 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

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 = BMP) matches with 95.45% similarity)

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

reference

Biochemistry 50:8497-8507 (2011)

PubMed id: 21870810

Mechanism of the orotidine 5'-monophosphate decarboxylase-catalyzed reaction: importance of residues in the orotate binding site.

V.Iiams, B.J.Desai, A.A.Fedorov, E.V.Fedorov, S.C.Almo, J.A.Gerlt.

ABSTRACT

No abstract given.