1O4M
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![BU of 1o4m by Molmil](/molmil-images/mine/1o4m) | CRYSTAL STRUCTURE OF SH2 IN COMPLEX WITH MALONICACID. | Descriptor: | MALONIC ACID, PROTO-ONCOGENE TYROSINE-PROTEIN KINASE SRC | Authors: | Lange, G, Loenze, P, Liesum, A. | Deposit date: | 2003-06-15 | Release date: | 2004-02-17 | Last modified: | 2023-08-16 | Method: | X-RAY DIFFRACTION (1.6 Å) | Cite: | Requirements for specific binding of low affinity inhibitor fragments to the SH2 domain of (pp60)Src are identical to those for high affinity binding of full length inhibitors. J.Med.Chem., 46, 2003
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1O42
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![BU of 1o42 by Molmil](/molmil-images/mine/1o42) | CRYSTAL STRUCTURE OF SH2 IN COMPLEX WITH RU81843. | Descriptor: | N-ACETYL-N-[1-(1,1'-BIPHENYL-4-YLMETHYL)-2-OXOAZEPAN-3-YL]-O-PHOSPHONOTYROSINAMIDE, PROTO-ONCOGENE TYROSINE-PROTEIN KINASE SRC | Authors: | Lange, G, Loenze, P, Liesum, A. | Deposit date: | 2003-06-15 | Release date: | 2004-02-17 | Last modified: | 2023-08-16 | Method: | X-RAY DIFFRACTION (1.7 Å) | Cite: | Requirements for specific binding of low affinity inhibitor fragments to the SH2 domain of (pp60)Src are identical to those for high affinity binding of full length inhibitors. J.Med.Chem., 46, 2003
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1O4E
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![BU of 1o4e by Molmil](/molmil-images/mine/1o4e) | CRYSTAL STRUCTURE OF SH2 IN COMPLEX WITH RU78299. | Descriptor: | 2,6-DIFORMYL-4-METHYLPHENYL DIHYDROGEN PHOSPHATE, PROTO-ONCOGENE TYROSINE-PROTEIN KINASE SRC | Authors: | Lange, G, Loenze, P, Liesum, A. | Deposit date: | 2003-06-15 | Release date: | 2004-02-17 | Last modified: | 2023-08-16 | Method: | X-RAY DIFFRACTION (2 Å) | Cite: | Requirements for specific binding of low affinity inhibitor fragments to the SH2 domain of (pp60)Src are identical to those for high affinity binding of full length inhibitors. J.Med.Chem., 46, 2003
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1O4R
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![BU of 1o4r by Molmil](/molmil-images/mine/1o4r) | CRYSTAL STRUCTURE OF SH2 IN COMPLEX WITH RU78783. | Descriptor: | (PHENYL-PHOSPHONO-METHYL)-PHOSPHONIC ACID, PROTO-ONCOGENE TYROSINE-PROTEIN KINASE SRC | Authors: | Lange, G, Loenze, P, Liesum, A. | Deposit date: | 2003-06-15 | Release date: | 2004-02-17 | Last modified: | 2023-08-16 | Method: | X-RAY DIFFRACTION (1.5 Å) | Cite: | Requirements for specific binding of low affinity inhibitor fragments to the SH2 domain of (pp60)Src are identical to those for high affinity binding of full length inhibitors. J.Med.Chem., 46, 2003
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1O4O
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![BU of 1o4o by Molmil](/molmil-images/mine/1o4o) | CRYSTAL STRUCTURE OF SH2 IN COMPLEX WITH PHENYLPHOSPHATE. | Descriptor: | PHENYL DIHYDROGEN PHOSPHATE, PROTO-ONCOGENE TYROSINE-PROTEIN KINASE SRC | Authors: | Lange, G, Loenze, P, Liesum, A. | Deposit date: | 2003-06-15 | Release date: | 2004-02-17 | Last modified: | 2023-08-16 | Method: | X-RAY DIFFRACTION (1.7 Å) | Cite: | Requirements for specific binding of low affinity inhibitor fragments to the SH2 domain of (pp60)Src are identical to those for high affinity binding of full length inhibitors. J.Med.Chem., 46, 2003
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1O41
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![BU of 1o41 by Molmil](/molmil-images/mine/1o41) | CRYSTAL STRUCTURE OF SH2 IN COMPLEX WITH RU78300. | Descriptor: | 2-FORMYL-6-METHOXYPHENYL DIHYDROGEN PHOSPHATE, PROTO-ONCOGENE TYROSINE-PROTEIN KINASE SRC | Authors: | Lange, G, Loenze, P, Liesum, A. | Deposit date: | 2003-06-15 | Release date: | 2004-02-17 | Last modified: | 2023-08-16 | Method: | X-RAY DIFFRACTION (1.7 Å) | Cite: | Requirements for specific binding of low affinity inhibitor fragments to the SH2 domain of (pp60)Src are identical to those for high affinity binding of full length inhibitors. J.Med.Chem., 46, 2003
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1O47
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![BU of 1o47 by Molmil](/molmil-images/mine/1o47) | CRYSTAL STRUCTURE OF SH2 IN COMPLEX WITH RU82209. | Descriptor: | N-ACETYL-N-[1-(1,1'-BIPHENYL-4-YLMETHYL)-2-OXOAZEPAN-3-YL]-4-[DIFLUORO(PHOSPHONO)METHYL]PHENYLALANINAMIDE, PROTO-ONCOGENE TYROSINE-PROTEIN KINASE SRC | Authors: | Lange, G, Loenze, P, Liesum, A. | Deposit date: | 2003-06-15 | Release date: | 2004-02-17 | Last modified: | 2023-08-16 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Requirements for specific binding of low affinity inhibitor fragments to the SH2 domain of (pp60)Src are identical to those for high affinity binding of full length inhibitors. J.Med.Chem., 46, 2003
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1O46
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![BU of 1o46 by Molmil](/molmil-images/mine/1o46) | CRYSTAL STRUCTURE OF SH2 IN COMPLEX WITH RU90395. | Descriptor: | 2-{4-[2-ACETYLAMINO-2-(1-BIPHENYL-4-YLMETHYL-2-OXO-AZEPAN-3-YLCARBAMOYL)-ETHYL]-2-METHOXYCARBONYL-PHENYL}-2-FLUORO-MALONIC ACID, PROTO-ONCOGENE TYROSINE-PROTEIN KINASE SRC | Authors: | Lange, G, Loenze, P, Liesum, A. | Deposit date: | 2003-06-15 | Release date: | 2004-02-17 | Last modified: | 2023-08-16 | Method: | X-RAY DIFFRACTION (2 Å) | Cite: | Requirements for specific binding of low affinity inhibitor fragments to the SH2 domain of (pp60)Src are identical to those for high affinity binding of full length inhibitors. J.Med.Chem., 46, 2003
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1O4B
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![BU of 1o4b by Molmil](/molmil-images/mine/1o4b) | CRYSTAL STRUCTURE OF SH2 IN COMPLEX WITH RU83876. | Descriptor: | N-ACETYL-N-[1-(1,1'-BIPHENYL-4-YLMETHYL)-2-OXOAZEPAN-3-YL]-3,4-DIPHOSPHONOPHENYLALANINAMIDE, PROTO-ONCOGENE TYROSINE-PROTEIN KINASE SRC | Authors: | Lange, G, Loenze, P, Liesum, A. | Deposit date: | 2003-06-15 | Release date: | 2004-02-17 | Last modified: | 2023-08-16 | Method: | X-RAY DIFFRACTION (1.85 Å) | Cite: | Requirements for specific binding of low affinity inhibitor fragments to the SH2 domain of (pp60)Src are identical to those for high affinity binding of full length inhibitors. J.Med.Chem., 46, 2003
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1O44
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![BU of 1o44 by Molmil](/molmil-images/mine/1o44) | Crystal structure of sh2 in complex with ru85052 | Descriptor: | 2-{4-[2-ACETYLAMINO-2-(1-BIPHENYL-4-YLMETHYL-2-OXO-AZEPAN-3-YLCARBAMOYL)-ETHYL]-2-CARBOXY-PHENYL}-MALONIC ACID, PROTO-ONCOGENE TYROSINE-PROTEIN KINASE SRC | Authors: | Lange, G, Loenze, P, Liesum, A. | Deposit date: | 2003-06-15 | Release date: | 2004-02-17 | Last modified: | 2023-08-16 | Method: | X-RAY DIFFRACTION (1.7 Å) | Cite: | Requirements for specific binding of low affinity inhibitor fragments to the SH2 domain of (pp60)Src are identical to those for high affinity binding of full length inhibitors. J.Med.Chem., 46, 2003
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