1tic

CONFORMATIONAL LABILITY OF LIPASES OBSERVED IN THE ABSENCE OF AN OIL-WATER INTERFACE: CRYSTALLOGRAPHIC STUDIES OF ENZYMES FROM THE FUNGI HUMICOLA LANUGINOSA AND RHIZOPUS DELEMARCONFORMATIONAL LABILITY OF LIPASES OBSERVED IN THE ABSENCE OF AN OIL-WATER INTERFACE: CRYSTALLOGRAPHIC STUDIES OF ENZYMES FROM THE FUNGI HUMICOLA LANUGINOSA AND RHIZOPUS DELEMAR

1tic is a 2 chain structure with sequence from Rhizopus arrhizus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.6Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

LIP_RHIOR Hydrolyzes ester bonds of triglycerides as well as of their derived partial glycerides with a strong 1,3-positional specificity.^[1]

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

↑ Ben Salah A, Sayari A, Verger R, Gargouri Y. Kinetic studies of Rhizopus oryzae lipase using monomolecular film technique. Biochimie. 2001 Jun;83(6):463-9. PMID:11506890