2cht

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CRYSTAL STRUCTURES OF THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS AND ITS COMPLEX WITH A TRANSITION STATE ANALOGCRYSTAL STRUCTURES OF THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS AND ITS COMPLEX WITH A TRANSITION STATE ANALOG

Structural highlights

2cht is a 12 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AROH_BACSU Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Gray JV, Golinelli-Pimpaneau B, Knowles JR. Monofunctional chorismate mutase from Bacillus subtilis: purification of the protein, molecular cloning of the gene, and overexpression of the gene product in Escherichia coli. Biochemistry. 1990 Jan 16;29(2):376-83. PMID:2105742

2cht, resolution 2.20Å

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OCA
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