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2JJI
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ENDOTHIAPEPSIN IN COMPLEX WITH A GEM-DIOL INHIBITOR.
Descriptor:ENDOTHIAPEPSIN, N~2~-[(2R)-2-benzyl-3-(tert-butylsulfonyl)propanoyl]-N-{(1R)-1-(cyclohexylmethyl)-3,3-difluoro-2,2-dihydroxy-4-[(2-morpholin-4-ylethyl)amino]-4-oxobutyl}-3-(1H-imidazol-3-ium-4-yl)-L-alaninamide, SULFATE ION
Authors:Coates, L., Tuan, H.-F., Tomanicek, S.J., Kovalevsky, A., Mustyakimov, M., Erskine, P., Cooper, J.
Deposit date:2008-04-09
Release date:2008-05-27
Last modified:2018-04-04
Method:X-RAY DIFFRACTION (1.57 Å)
Cite:The Catalytic Mechanism of an Aspartic Proteinase Explored with Neutron and X-Ray Diffraction
J.Am.Chem.Soc., 130, 2008
2JJJ
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ENDOTHIAPEPSIN IN COMPLEX WITH A GEM-DIOL INHIBITOR.
Descriptor:ENDOTHIAPEPSIN, N~2~-[(2R)-2-benzyl-3-(tert-butylsulfonyl)propanoyl]-N-{(1R)-1-(cyclohexylmethyl)-3,3-difluoro-2,2-dihydroxy-4-[(2-morpholin-4-ylethyl)amino]-4-oxobutyl}-3-(1H-imidazol-3-ium-4-yl)-L-alaninamide, SULFATE ION
Authors:Coates, L., Tuan, H.-F., Tomanicek, S.J., Kovalevsky, A., Mustyakimov, M., Erskine, P., Cooper, J.
Deposit date:2008-04-09
Release date:2008-05-27
Last modified:2013-09-25
Method:X-RAY DIFFRACTION (1 Å)
Cite:The Catalytic Mechanism of an Aspartic Proteinase Explored with Neutron and X-Ray Diffraction
J.Am.Chem.Soc., 130, 2008
2VS2
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NEUTRON DIFFRACTION STRUCTURE OF ENDOTHIAPEPSIN IN COMPLEX WITH A GEM- DIOL INHIBITOR.
Descriptor:ENDOTHIAPEPSIN, N~2~-[(2R)-2-benzyl-3-(tert-butylsulfonyl)propanoyl]-N-{(1R)-1-(cyclohexylmethyl)-3,3-difluoro-2,2-dihydroxy-4-[(2-morpholin-4-ylethyl)amino]-4-oxobutyl}-3-(1H-imidazol-3-ium-4-yl)-L-alaninamide
Authors:Coates, L., Tuan, H.-F., Tomanicek, S., Kovalevsky, A., Mustyakimov, M., Erskine, P., Cooper, J.
Deposit date:2008-04-17
Release date:2008-05-27
Last modified:2018-11-14
Method:NEUTRON DIFFRACTION (2 Å)
Cite:The Catalytic Mechanism of an Aspartic Proteinase Explored with Neutron and X-Ray Diffraction
J.Am.Chem.Soc., 130, 2008
2BJI
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HIGH RESOLUTION STRUCTURE OF MYO-INOSITOL MONOPHOSPHATASE, THE TARGET OF LITHIUM THERAPY
Descriptor:INOSITOL-1(OR 4)-MONOPHOSPHATASE, MAGNESIUM ION
Authors:Gill, R., Mohammed, F., Badyal, R., Coates, L., Erskine, P., Thompson, D., Cooper, J., Gore, M., Wood, S.
Deposit date:2005-02-03
Release date:2005-02-11
Last modified:2018-02-28
Method:X-RAY DIFFRACTION (1.24 Å)
Cite:High-resolution structure of myo-inositol monophosphatase, the putative target of lithium therapy.
Acta Crystallogr. D Biol. Crystallogr., 61, 2005
2WYX
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NEUTRON STRUCTURE OF A CLASS A BETA-LACTAMASE TOHO-1 E166A R274N R276N TRIPLE MUTANT
Descriptor:BETA-LACTAMSE TOHO-1
Authors:Tomanicek, S.J., Blakeley, M.P., Cooper, J., Chen, Y., Afonine, P., Coates, L.
Deposit date:2009-11-20
Release date:2010-01-12
Last modified:2018-05-09
Method:NEUTRON DIFFRACTION (2.1 Å)
Cite:Neutron Diffraction Studies of a Class a Beta-Lactamase Toho-1 E166A R274N R276N Triple Mutant
J.Mol.Biol., 396, 2010
2XQZ
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NEUTRON STRUCTURE OF THE PERDEUTERATED TOHO-1 R274N R276N DOUBLE MUTANT BETA-LACTAMASE
Descriptor:BETA-LACTAMSE TOHO-1
Authors:Tomanicek, S.J., Wang, K.K., Weiss, K.L., Blakeley, M.P., Cooper, J., Chen, Y., Coates, L.
Deposit date:2010-09-08
Release date:2010-12-22
Last modified:2018-01-31
Method:NEUTRON DIFFRACTION (2.1 Å)
Cite:The Active Site Protonation States of Perdeuterated Toho-1 Beta-Lactamase Determined by Neutron Diffraction Support a Role for Glu166 as the General Base in Acylation.
FEBS Lett., 585, 2011
2XR0
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ROOM TEMPERATURE X-RAY STRUCTURE OF THE PERDEUTERATED TOHO-1 R274N R276N DOUBLE MUTANT BETA-LACTAMASE
Descriptor:TOHO-1 BETA-LACTAMASE, SULFATE ION
Authors:Tomanicek, S.J., Wang, K.K., Weiss, K.L., Blakeley, M.P., Cooper, J., Chen, Y., Coates, L.
Deposit date:2010-09-08
Release date:2010-12-22
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (2.2 Å)
Cite:The Active Site Protonation States of Perdeuterated Toho-1 Beta-Lactamase Determined by Neutron Diffraction Support a Role for Glu166 as the General Base in Acylation.
FEBS Lett., 585, 2011
2ER6
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THE STRUCTURE OF A SYNTHETIC PEPSIN INHIBITOR COMPLEXED WITH ENDOTHIAPEPSIN.
Descriptor:ENDOTHIAPEPSIN, H-256 peptide
Authors:Cooper, J.B., Foundling, S.I., Szelke, M., Blundell, T.L.
Deposit date:1990-10-13
Release date:1991-01-15
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (2 Å)
Cite:The structure of a synthetic pepsin inhibitor complexed with endothiapepsin
Eur.J.Biochem., 169, 1987
1EED
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X-RAY CRYSTALLOGRAPHIC ANALYSIS OF INHIBITION OF ENDOTHIAPEPSIN BY CYCLOHEXYL RENIN INHIBITORS
Descriptor:ENDOTHIAPEPSIN, (2S)-2-[[(3S,4S)-5-cyclohexyl-4-[[(4S,5S)-5-[(2-methylpropan-2-yl)oxycarbonylamino]-4-oxidanyl-6-phenyl-hexanoyl]amino]-3-oxidanyl-pentanoyl]amino]-4-methyl-pentanoic acid
Authors:Blundell, T.L., Frazao, C., Cooper, J.B.
Deposit date:1992-06-15
Release date:1994-01-31
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (2 Å)
Cite:X-ray crystallographic analysis of inhibition of endothiapepsin by cyclohexyl renin inhibitors.
Biochemistry, 31, 1992
3ER5
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THE ACTIVE SITE OF ASPARTIC PROTEINASES
Descriptor:ENDOTHIAPEPSIN, H-189
Authors:Bailey, D., Veerapandian, B., Cooper, J., Szelke, M., Blundell, T.L.
Deposit date:1991-01-05
Release date:1991-04-15
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:X-ray-crystallographic studies of complexes of pepstatin A and a statine-containing human renin inhibitor with endothiapepsin.
Biochem.J., 289 ( Pt 2), 1993
1B5F
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NATIVE CARDOSIN A FROM CYNARA CARDUNCULUS L.
Descriptor:PROTEIN (CARDOSIN A), N-ACETYL-D-GLUCOSAMINE, ALPHA-L-FUCOSE, ...
Authors:Frazao, C., Bento, I., Carrondo, M.A.
Deposit date:1999-01-06
Release date:1999-01-13
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (1.72 Å)
Cite:Crystal structure of cardosin A, a glycosylated and Arg-Gly-Asp-containing aspartic proteinase from the flowers of Cynara cardunculus L.
J.Biol.Chem., 274, 1999
4ER4
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HIGH-RESOLUTION X-RAY ANALYSES OF RENIN INHIBITOR-ASPARTIC PROTEINASE COMPLEXES
Descriptor:ENDOTHIAPEPSIN, H-142
Authors:Foundling, S.I., Watson, F.E., Szelke, M., Blundell, T.L.
Deposit date:1991-01-05
Release date:1991-04-15
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (2.1 Å)
Cite:High resolution X-ray analyses of renin inhibitor-aspartic proteinase complexes.
Nature, 327, 1987