Literature summary extracted from

Harris, M.S.; Bock, J.H.; Choi, G.; Cialdella, J.S.; Curry, K.A.; Deibel, M.R., Jr.; Jacobsen, E.J.; Marshall, V.P.; Murray, R.W., Jr.; Vosters, A.F.; Wolfe, C.L.; Yem, A.W.; Baldwin, E.T.
Co-crystallization of Staphylococcus aureus peptide deformylase (PDF) with potent inhibitors (2002), Acta Crystallogr. Sect. D, 58, 2153-2156.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
3.5.1.88	sitting-drop vapour-diffusion method. Preparation of diffraction-quality Se-Met crystals of peptide deformylase that belong to space group C222(1) with unit cell parameters of a = 94.1 A, b = 121.9 A, c = 47.6 A, 1.9 resolution. Preparation of crystals with the inhibitors thiorphan, actinonin and PONU-172550. The thiorphan and actinonin co-crystals belong to space group C222(1). Repeated attempts to generate a complex structure of peptide deformylase with PNU-172550 from the orthorhombic space group are unsuccessful. Crystallization screening identifies an alternate C2 crystal form with unit cell dimensions of a = 93.4, b = 42.5, c = 104.1 A, beta = 93°	Staphylococcus aureus

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.5.1.88	Staphylococcus aureus	-	-	-

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Release 2023.1 (January 2023)