PDBsum entry 1ecm

Chorismate mutase

PDB id: 1ecm

Contents

Protein chains

91 a.a. *

Ligands

TSA ×2

Waters ×77

* Residue conservation analysis

PDB id:

1ecm

Name:

Chorismate mutase

Title:

Atomic structure of the buried catalytic pocket of escherichia coli chorismate mutase

Structure:

Endo-oxabicyclic transition state analogue. Chain: a, b. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 562. Strain: pjs47. Cell_line: nk6024

Biol. unit:

Tetramer (from PQS)

Resolution:

2.20Å R-factor: 0.192 R-free: 0.231

Authors:

J.Clardy,A.Y.Lee

Key ref:

A.Y.Lee et al. (1995). Atomic-Structure of the buried catalytic pocket of escherichia-Coli chorismate mutase.. J am chem soc, 117, 3627-3628.

Date:

28-Nov-94 Release date: 01-Dec-95

Protein chains

P0A9J8  (PHEA_ECOLI) -  Bifunctional chorismate mutase/prephenate dehydratase from Escherichia coli (strain K12)

Seq: 386 a.a.

Struc: 91 a.a.

Enzyme reactions

• Enzyme class 1: E.C.4.2.1.51 - prephenate dehydratase.
• Pathway: Phenylalanine and Tyrosine Biosynthesis
• Reaction: prephenate + H⁺ = 3-phenylpyruvate + CO2 + H2O

prephenate + H(+) (Bound ligand (Het Group name = TSA) corresponds exactly) = 3-phenylpyruvate + CO2 + H2O

• Cofactor: Pyridoxal 5'-phosphate
• Enzyme class 2: E.C.5.4.99.5 - chorismate mutase.

Pathway:

• Reaction: chorismate = prephenate

chorismate (Bound ligand (Het Group name = TSA) corresponds exactly) = prephenate

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

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