2cb1

Crystal Structure of O-actetyl Homoserine Sulfhydrylase From Thermus Thermophilus HB8,OAH2.Crystal Structure of O-actetyl Homoserine Sulfhydrylase From Thermus Thermophilus HB8,OAH2.

Structural highlights 2cb1 is a 1 chain structure with sequence from Thermus thermophilus HB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN Function METY2_THET8 Catalyzes the conversion of O-acetyl-L-homoserine (OAH) into homocysteine in the methionine biosynthesis pathway. Has weak activity with O-acetyl-L-serine, O-phospho-L-serine, L-serine, O-succinyl-L-homoserine and L-homoserine. Shows a very low CTT gamma-synthase activity. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

spinqualitylabelsall models 2cb1, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image