1g6x

ULTRA HIGH RESOLUTION STRUCTURE OF BOVINE PANCREATIC TRYPSIN INHIBITOR (BPTI) MUTANT WITH ALTERED BINDING LOOP SEQUENCE

spinqualitylabelsall models 1g6x, resolution 0.86Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1g6x is a 1 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 0.86Å Ligands: EDO, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BPT1_BOVIN Inhibits trypsin, kallikrein, chymotrypsin, and plasmin. 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 crystal structure of a mutant of bovine pancreatic trypsin inhibitor has been refined to 0.86 A resolution using low-temperature synchrotron data. The variant contains three mutations in the binding loop (Thr11Ala, Pro13Ala, Lys15Arg) and an unrelated Met52Leu substitution. Refinement with anisotropic displacement parameters and with removal of main-chain stereochemical restraints converged with R = 0.1035. The use of full-matrix refinement provided an estimate of the variances in the derived parameters. Some stereochemical parameters, such as the planarity of the peptide group and the value of the N-C(alpha)-C angle, show a wide spread, suggesting that the standard values used as restraints in protein structure refinements may not always be entirely appropriate. Comparison with the recently determined room-temperature structure of the same mutant at 1.42 A resolution confirms the previous observations and provides new details, such as a double conformation of the main chain at Leu29 and at Gly56-Gly57, a high proportion (over 20%) of residues in double conformations, correlation of disorder through lattice contacts and the positions of H atoms, including those in water molecules, and their involvement in C-H...O and N-H...pi hydrogen bonds. Ultrahigh-resolution structure of a BPTI mutant.,Addlagatta A, Krzywda S, Czapinska H, Otlewski J, Jaskolski M Acta Crystallogr D Biol Crystallogr. 2001 May;57(Pt 5):649-63. Epub 2001, Apr 24. PMID:11320305 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also BPTI 3D structures

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