The crystal structure of a Lipase-esterase related protein from Clostridium acetobutylicum ATCC 824

Midwest Center for Structural Genomics (MCSG)

SNA(MSE)LHYVHVGNKKSPNTLLFVHGSGCNLKIFGELEKYLEDYNCILLDLKGHGESKGQCPSTVYGYIDNVANFITN
SEVTKHQKNITLIGYS(MSE)GGAIVLGVALKKLPNVRKVVSLSGGARFDKLDKDF(MSE)EKIYHNQLDNNYLLECIGG
IDNPLSEKYFETLEKDPDI(MSE)INDLIACKLIDLVDNLKNIDIPVKAIVAKDELLTLVEYSEIIKKEVENSELKIFET
GKHFLLVVNAKGVAEEIKNFI

SNAMLHYVHVGNKKSPNTLLFVHGSGCNLKIFGELEKYLEDYNCILLDLKGHGESKGQCPSTVYGYIDNVANFITNSEVT
KHQKNITLIGYSMGGAIVLGVALKKLPNVRKVVSLSGGARFDKLDKDFMEKIYHNQLDNNYLLECIGGIDNPLSEKYFET
LEKDPDIMINDLIACKLIDLVDNLKNIDIPVKAIVAKDELLTLVEYSEIIKKEVENSELKIFETGKHFLLVVNAKGVAEE
IKNFI

0.2M LiCl
20% PEG3350, VAPOR DIFFUSION, SITTING DROP, temperature 289K

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

Authors state that the biological assembly is experimentally unknown. From molecular packing, the molecule is expected to be a monomer.

APC60309, Lipase-esterase related protein, Clostridium acetobutylicum ATCC 824, structural genomics, PSI-2, midwest center for structural genomics, MCSG, Protein Structure Initiative, unknown function

MLHYVHVGNKKSPNTLLFVHGSGCNLKIFGELEKYLEDYNCILLDLKGHGESKGQCPSTVYGYIDNVANFITNSEVTKHQ
KNITLIGYSMGGAIVLGVALKKLPNVRKVVSLSGGARFDKLDKDFMEKIYHNQLDNNYLLECIGGIDNPLSEKYFETLEK
DPDIMINDLIACKLIDLVDNLKNIDIPVKAIVAKDELLTLVEYSEIIKKEVENSELKIFETGKHFLLVVNAKGVAEEIKN
FI