Your request to link to rcsb for Alpha-amylase

  • 1CPU: subsite mapping of the active site of human pancreatic alpha-amylase using substrates, the pharmacological inhibitor acarbose, and an active site variant (10.1021/BI9921182 )
  • 1DHK: structure of porcine pancreatic alpha-amylase (10.1016/S0969-2126(96)00151-7 )
  • 1HNY: the structure of human pancreatic alpha-amylase at 1.8 angstroms resolution and comparisons with related enzymes
  • 1HX0: structure of pig pancreatic alpha-amylase complexed with the "truncate" acarbose molecule (pseudotrisaccharide) (10.1021/BI0102050 )
  • 1JFH: structure of a pancreatic alpha-amylase bound to a substrate analogue at 2.03 angstrom resolution
  • 1JXJ: role of mobile loop in the mechanism of human salivary amylase (10.1111/J.1432-1033.2004.04182.X )
  • 1JXK: role of ethe mobile loop in the mehanism of human salivary amylase (10.1016/S0022-2836(02)01326-8 )
  • 1KB3: three dimensional structure analysis of the r195a variant of human pancreatic alpha amylase (10.1021/BI0115636 )
  • 1KBB: mechanistic analyses of catalysis in human pancreatic alpha-amylase: detailed kinetic and structural studies of mutants of three conserved carboxylic acids (10.1021/BI011821Z )
  • 1KBK: mechanistic analyses of catalysis in human pancreatic alpha-amylase: detailed kinetic and structural studies of mutants of three conserved carboxylic acids (10.1021/BI011821Z )
  • 1KGU: three dimensional structure analysis of the r337a variant of human pancreatic alpha-amylase (10.1021/BI0115636 )
  • 1KGW: three dimensional structure analysis of the r337q variant of human pancreatic alpha-mylase (10.1021/BI0115636 )
  • 1KGX: three dimensional structure analysis of the r195q variant of human pancreatic alpha amylase (10.1021/BI0115636 )
  • 1KXQ: camelid vhh domain in complex with porcine pancreatic alpha-amylase (10.1074/JBC.M202327200 )
  • 1KXT: camelid vhh domains in complex with porcine pancreatic alpha-amylase (10.1074/JBC.M202327200 )
  • 1KXV: camelid vhh domains in complex with porcine pancreatic alpha-amylase (10.1074/JBC.M202327200 )
  • 1MFU: probing the role of a mobile loop in human salivary amylase: structural studies on the loop-deleted mutant (10.1016/S0022-2836(02)01326-8 )
  • 1MFV: probing the role of a mobile loop in human slaivary amylase: structural studies on the loop-deleted enzyme (10.1016/S0022-2836(02)01326-8 )
  • 1NM9: crystal structure of recombinant human salivary amylase mutant w58a (10.1111/J.1432-1033.2004.04182.X )
  • 1OSE: porcine pancreatic alpha-amylase complexed with acarbose (10.1111/J.1432-1033.1996.0561Z.X )
  • 1PIF: pig alpha-amylase (10.1006/JMBI.1996.0410 )
  • 1PIG: pig pancreatic alpha-amylase complexed with the oligosaccharide v-1532 (10.1006/JMBI.1996.0410 )
  • 1PPI: the active center of a mammalian alpha-amylase. the structure of the complex of a pancreatic alpha-amylase with a carbohydrate inhibitor refined to 2.2 angstroms resolution (10.1021/BI00186A031 )
  • 1Q4N: structural studies of phe256trp of human salivary alpha-amylase: implications for the role of a conserved water molecule and its associated chain in enzyme activity 25-jan-05 1q4n 1 title (10.1016/J.ABB.2003.10.007 )
  • 1SMD: human salivary amylase (10.1107/S0907444995014119 )
  • 1U2Y: in situ extension as an approach for identifying novel alpha-amylase inhibitors, structure containing d-gluconhydroximo-1,5-lactam (10.1074/JBC.M406804200 )
  • 1U30: in situ extension as an approach for identifying novel alpha-amylase inhibitors, structure containing maltosyl-alpha (1,4)-d- gluconhydroximo-1,5-lactam (10.1074/JBC.M406804200 )
  • 1U33: in situ extension as an approach for identifying novel alpha-amylase inhibitors (10.1074/JBC.M406804200 )
  • 1UA3: crystal structure of the pig pancreatic a-amylase complexed with malto-oligosaccharides (10.1023/A:1025072520607 )
  • 1VAH: crystal structure of the pig pancreatic-amylase complexed with r- nitrophenyl-a-d-maltoside (10.1023/B:JOPC.0000039552.94529.95 )
  • 1WO2: crystal structure of the pig pancreatic alpha-amylase complexed with malto-oligosaacharides under the effect of the chloride ion (10.1021/BI048201T )
  • 1XCW: acarbose rearrangement mechanism implied by the kinetic and structural analysis of human pancreatic alpha-amylase in complex with analogues and their elongated counterparts (10.1021/BI048334E )
  • 1XCX: acarbose rearrangement mechanism implied by the kinetic and structural analysis of human pancreatic alpha-amylase in complex with analogues and their elongated counterparts (10.1021/BI048334E )
  • 1XD0: acarbose rearrangement mechanism implied by the kinetic and structural analysis of human pancreatic alpha-amylase in complex with analogues and their elongated counterparts (10.1021/10.1021/BI048334E )
  • 1XD1: acarbose rearrangement mechanism implied by the kinetic and structural analysis of human pancreatic alpha-amylase in complex with analogues and their elongated counterparts (10.1021/BI048334E )
  • 1XGZ: structure of the n298s variant of human pancreatic alpha-amylase (10.1110/PS.041079305 )
  • 1XH0: structure of the n298s variant of human pancreatic alpha-amylase complexed with acarbose (10.1110/PS.041079305 )
  • 1XH1: structure of the n298s variant of human pancreatic alpha-amylase complexed with chloride (10.1110/PS.041079305 )
  • 1XH2: structure of the n298s variant of human pancreatic alpha-amylase complexed with chloride and acarbose (10.1110/PS.041079305 )
  • 1XV8: crystal structure of human salivary alpha-amylase dimer
  • 1Z32: structure-function relationships in human salivary alpha-amylase: role of aromatic residues
  • 2CPU: subsite mapping of the active site of human pancreatic alpha-amylase using substrates, the pharmacological inhibitor acarbose, and an active site variant (10.1021/BI9921182 )
  • 2QMK: human pancreatic alpha-amylase complexed with nitrite (10.1021/BI701652T )
  • 2QV4: human pancreatic alpha-amylase complexed with nitrite and acarbose (10.1021/BI701652T )
  • 3BAI: human pancreatic alpha amylase with bound nitrate (10.1021/BI701652T )
  • 3BAJ: human pancreatic alpha-amylase in complex with nitrate and acarbose (10.1021/BI701652T )
  • 3BAK: n298s mutant of human pancreatic alpha-amylase in complex with nitrate (10.1021/BI701652T )
  • 3BAW: human pancreatic alpha-amylase complexed with azide (10.1021/BI701652T )
  • 3BAX: n298s variant of human pancreatic alpha-amylase in complex with azide (10.1021/BI701652T )
  • 3BAY: n298s variant of human pancreatic alpha-amylase in complex with nitrate and acarbose (10.1021/BI701652T )
  • 3BLK: role of aromatic residues in starch binding (10.2478/S11756-008-0163-3 )
  • 3BLP: role of aromatic residues in human salivary alpha-amylase (10.2478/S11756-008-0163-3 )
  • 3CPU: subsite mapping of the active site of human pancreatic alpha-amylase using substrates, the pharmacological inhibitor acarbose, and an active site variant (10.1021/BI9921182 )
  • 3DHP: probing the role of aromatic residues at the secondary saccharide binding sites of human salivary alpha-amylase in substrate hydrolysis and bacterial binding
  • 3IJ7: directed 'in situ' elongation as a strategy to characterize the covalent glycosyl-enzyme catalytic intermediate of human pancreatic a-amylase (10.1021/BI901400P )
  • 3IJ8: directed 'in situ' elongation as a strategy to characterize the covalent glycosyl-enzyme catalytic intermediate of human pancreatic a-amylase (10.1021/BI901400P )
  • 3IJ9: directed 'in situ' elongation as a strategy to characterize the covalent glycosyl-enzyme catalytic intermediate of human pancreatic a-amylase (10.1021/BI901400P )
  • 3L2L: x-ray crystallographic analysis of pig pancreatic alpha-amylase with limit dextrin and oligosaccharide (10.1021/BI902183W )
  • 3L2M: x-ray crystallographic analysis of pig pancreatic alpha-amylase with alpha-cyclodextrin (10.1021/BI902183W )
  • 3OLD: crystal structure of alpha-amylase in complex with acarviostatin i03 (10.1016/J.JSB.2010.11.020 )
  • 3OLE: structures of human pancreatic alpha-amylase in complex with acarviostatin ii03 (10.1016/J.JSB.2010.11.020 )
  • 3OLG: structures of human pancreatic alpha-amylase in complex with acarviostatin iii03 (10.1016/J.JSB.2010.11.020 )
  • 3OLI: structures of human pancreatic alpha-amylase in complex with acarviostatin iv03 (10.1016/J.JSB.2010.11.020 )
  • 4GQQ: human pancreatic alpha-amylase with bound ethyl caffeate (10.1021/JM301273U )
  • 4GQR: human pancreatic alpha-amylase in complex with myricetin (10.1021/JM301273U )
  • 4W93: human pancreatic alpha-amylase in complex with montbretin a (10.1038/NCHEMBIO.1865 )
  • 4X0N: porcine pancreatic alpha-amylase in complex with helianthamide, a novel proteinaceous inhibitor
  • 4X9Y: wild-type human pancreatic alpha-amylase at true atomic resolution (1.07 a)
  • 5E0F: human pancreatic alpha-amylase in complex with mini-montbretin a
  • 5EMY: human pancreatic alpha-amylase in complex with the mechanism based inactivator glucosyl epi-cyclophellitol (10.1002/1873-3468.12143 )
  • 5KEZ: selective and potent inhibition of the glycosidase human amylase by the short and extremely compact peptide piha from mrna display (10.1016/J.CHEMBIOL.2017.02.001 )
  • 5TD4: starch binding sites on the human pancreatic alpha amylase d300n variant complexed with an octaose substrate. (10.1021/ACS.BIOCHEM.6B00992 )
  • 5U3A: ultra high resolution crystal structure of human pancreatic alpha amylase (10.1021/ACSCHEMBIO.9B00290 )
  • 5VA9: human pancreatic alpha amylase in complex with peptide inhibitor piha- l5(d10y) (10.1021/ACSCHEMBIO.9B00290 )
  • 6OBX: montbretin a analogue m10-mba in complex with human pancreatic alpha- amylase (10.1039/C9SC02610J )
  • 6OCN: montbretin a analogue m06-mba in complex with human pancreatic alpha- amylase (10.1039/C9SC02610J )
  • 6Z8L: alpha-amylase in complex with probe fragments (10.1039/D0SC04297H )