4add

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Structural and functional study of succinyl-ornithine transaminase from E. coliStructural and functional study of succinyl-ornithine transaminase from E. coli

Structural highlights

4add is a 4 chain structure with sequence from Escherichia coli BL21. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.45Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ASTC_ECOLI Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase.[1]

See Also

References

  1. ↑ Schneider BL, Kiupakis AK, Reitzer LJ. Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli. J Bacteriol. 1998 Aug;180(16):4278-86. PMID:9696779

4add, resolution 2.45Å

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OCA
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