PDBsum entry 4myd

Lyase

PDB id: 4myd

Contents

Protein chains

252 a.a.

Ligands

164 ×2

Waters ×797

PDB id:

4myd

Name:

Lyase

Title:

1.37 angstrom crystal structure of e. Coli 2-succinyl-6-hydroxy-2,4- cyclohexadiene-1-carboxylate synthase (menh) in complex with shchc

Structure:

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase. Chain: a, b, c. Synonym: shchc synthase. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: b2263, jw2258, menh, yfbb. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.37Å R-factor: 0.130 R-free: 0.166

Authors:

Y.Sun,S.Yin,Y.Feng,J.Li,J.Zhou,C.Liu,G.Zhu,Z.Guo

Key ref:

Y.Sun et al. (2014). Molecular basis of the general base catalysis of an α/β-hydrolase catalytic triad. J Biol Chem, 289, 15867-15879. PubMed id: 24737327 DOI: 10.1074/jbc.M113.535641

Date:

27-Sep-13 Release date: 23-Apr-14

Protein chains

P37355  (MENH_ECOLI) -  2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase from Escherichia coli (strain K12)

Seq: 252 a.a.

Struc: 252 a.a.

Enzyme reactions

• Enzyme class: E.C.4.2.99.20 - 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase.
• Reaction: 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate = (1R,6R)-6-hydroxy-2-succinyl-cyclohexa-2,4-diene-1-carboxylate + pyruvate

5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate = (1R,6R)-6-hydroxy-2-succinyl-cyclohexa-2,4-diene-1-carboxylate (Bound ligand (Het Group name = 164) corresponds exactly) + pyruvate

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

Added reference

DOI no: 10.1074/jbc.M113.535641

J Biol Chem 289:15867-15879 (2014)

PubMed id: 24737327

Molecular basis of the general base catalysis of an α/β-hydrolase catalytic triad.

Y.Sun, S.Yin, Y.Feng, J.Li, J.Zhou, C.Liu, G.Zhu, Z.Guo.

ABSTRACT

No abstract given.