1bvn

PIG PANCREATIC ALPHA-AMYLASE IN COMPLEX WITH THE PROTEINACEOUS INHIBITOR TENDAMISTAT

spinqualitylabelsall models 1bvn, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1bvn is a 2 chain structure with sequence from Streptomyces tendae and Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, CL Activity: Alpha-amylase, with EC number 3.2.1.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [IAA_STRTE] Inhibits mammalian alpha-amylases specifically but has no action on plant and microbial alpha-amylases. Forms a tight stoichiometric 1:1 complex with alpha-amylase. 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 the complex formed between the 498 amino acid residue porcine pancreatic alpha-amylase (PPA) and the 74 amino acid residue inhibitor Tendamistat secreted from Streptomyces tendae, has been determined by multiple isomorphous replacement in a crystal of space group P6(5)22 (a = b = 77.7 A, c = 359.5 A). The model has been refined to an R-factor of 0.194 by Powell minimization applying strong energy constraints based on 17,964 independent reflections in the 7 to 2.5 A resolution range, and obeys standard geometry within 0.011 A in bond lengths and 1.78 degrees in bond angles. The final model consists of all 496 amino acid residues of PPA, 71 amino acid residues of Tendamistat (without the three N-terminal residues), one calcium ion, one chloride ion and 167 water molecules. PPA exhibits the same topological fold in the complex as the uncomplexed PPA recently published by others. About 30% of the water-accessible surface of Tendamistat is in contact with PPA. Four segments of the polypeptide chain, with a total of 15 amino acid residues, are involved in the binding. One segment containing the staggered side-chains of the triplet Trp18, Arg19, Tyr20, typical for this class of inhibitors, binds into the catalytic site. The other segments fill out the groove in the PPA molecule, which also binds the carbohydrate inhibitor acarbose and is assumed to be the substrate-binding region. This extended interaction between Tendamistat and alpha-amylase explains the very high inhibition constant of about 9 x 10(-12) M. The crystal structure of porcine pancreatic alpha-amylase in complex with the microbial inhibitor Tendamistat.,Wiegand G, Epp O, Huber R J Mol Biol. 1995 Mar 17;247(1):99-110. PMID:7897663 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Amylase 3D structures

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