1aks

CRYSTAL STRUCTURE OF THE FIRST ACTIVE AUTOLYSATE FORM OF THE PORCINE ALPHA TRYPSINCRYSTAL STRUCTURE OF THE FIRST ACTIVE AUTOLYSATE FORM OF THE PORCINE ALPHA TRYPSIN

Structural highlights 1aks is a 2 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TRYP_PIG Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The first crystal structure of an active autolysate form of porcine alpha-trypsin (APT), a two-chain molecule obtained from the limited autolysis of porcine beta-trypsin at position Lys145-Ser146, has been determined. APT crystallizes in space group P2(1)2(1)2(1) with one protein molecule in the asymmetric unit. The structure was solved by molecular replacement followed by refinement using X-PLOR to an R factor of 0.200 and an R(free) of 0.285 for 8.0-1.8 A data with r.m.s deviations from ideal values of 0.01 A and 1.7 degrees for bond lengths and bond angles, respectively. Comparison with inactive autolysate porcine epsilon-trypsin (EPT) and porcine beta-trypsin in complex with bittergourd trypsin inhibitor (MCT) revealed a small but systematic directional chain shift around the active-site residues from APT to EPT to MCT. The first structure at 1.8 A resolution of an active autolysate form of porcine alpha-trysoin.,Johnson A, Krishnaswamy S, Sundaram PV, Pattabhi V Acta Crystallogr D Biol Crystallogr. 1997 May 1;53(Pt 3):311-5. PMID:15299934 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Trypsin 3D structures

spinqualitylabelsall models 1aks, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image