1EAG
| Secreted aspartic proteinase (SAP2) from Candida albicans complexed with A70450 | Descriptor: | ASPARTIC PROTEINASE (SAP2 GENE PRODUCT), N-ethyl-N-[(4-methylpiperazin-1-yl)carbonyl]-D-phenylalanyl-N-[(1S,2S,4R)-4-(butylcarbamoyl)-1-(cyclohexylmethyl)-2-hydroxy-5-methylhexyl]-L-norleucinamide | Authors: | Cutfield, J.F, Cutfield, S.M. | Deposit date: | 1996-05-31 | Release date: | 1996-12-23 | Last modified: | 2012-01-18 | Method: | X-RAY DIFFRACTION (2.1 Å) | Cite: | The crystal structure of a major secreted aspartic proteinase from Candida albicans in complexes with two inhibitors. Structure, 3, 1995
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6OS4
| Calmodulin in complex with farnesyl cysteine methyl ester | Descriptor: | CALCIUM ION, Calmodulin-1, s-farnesyl-l-cysteine methyl ester | Authors: | Grant, B.M.M, Enomoto, M, Lee, K.Y, Back, S.I, Gebregiworgis, T, Ishiyama, N, Ikura, M, Marshall, C. | Deposit date: | 2019-05-01 | Release date: | 2020-04-08 | Last modified: | 2024-03-13 | Method: | X-RAY DIFFRACTION (2.05 Å) | Cite: | Calmodulin disrupts plasma membrane localization of farnesylated KRAS4b by sequestering its lipid moiety. Sci.Signal., 13, 2020
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2MSD
| NMR data-driven model of GTPase KRas-GNP tethered to a lipid-bilayer nanodisc | Descriptor: | 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE, Apolipoprotein A-I, GTPase KRas, ... | Authors: | Mazhab-Jafari, M, Stathopoulos, P, Marshall, C, Ikura, M. | Deposit date: | 2014-07-29 | Release date: | 2015-06-03 | Last modified: | 2019-12-11 | Method: | SOLUTION NMR | Cite: | Oncogenic and RASopathy-associated K-RAS mutations relieve membrane-dependent occlusion of the effector-binding site. Proc.Natl.Acad.Sci.USA, 112, 2015
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2MSE
| NMR data-driven model of GTPase KRas-GNP:ARafRBD complex tethered to a lipid-bilayer nanodisc | Descriptor: | 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE, Apolipoprotein A-I, GTPase KRas, ... | Authors: | Mazhab-Jafari, M, Stathopoulos, P, Marshall, C, Ikura, M. | Deposit date: | 2014-07-29 | Release date: | 2015-06-03 | Last modified: | 2019-12-11 | Method: | SOLUTION NMR | Cite: | Oncogenic and RASopathy-associated K-RAS mutations relieve membrane-dependent occlusion of the effector-binding site. Proc.Natl.Acad.Sci.USA, 112, 2015
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2MSC
| NMR data-driven model of GTPase KRas-GDP tethered to a lipid-bilayer nanodisc | Descriptor: | 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE, Apolipoprotein A-I, GTPase KRas, ... | Authors: | Mazhab-Jafari, M, Stathopoulos, P, Marshall, C, Ikura, M. | Deposit date: | 2014-07-29 | Release date: | 2015-06-03 | Last modified: | 2019-12-11 | Method: | SOLUTION NMR | Cite: | Oncogenic and RASopathy-associated K-RAS mutations relieve membrane-dependent occlusion of the effector-binding site. Proc.Natl.Acad.Sci.USA, 112, 2015
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