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1D27
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BU of 1d27 by Molmil
HIGH-RESOLUTION STRUCTURE OF A MUTAGENIC LESION IN DNA
分子名称: DNA (5'-D(*CP*GP*CP*(6OG)P*AP*AP*TP*TP*TP*GP*CP*G)-3')
著者Leonard, G.A, Thomson, J, Watson, W.P, Brown, T.
登録日1991-04-22
公開日1992-04-07
最終更新日2024-02-07
実験手法X-RAY DIFFRACTION (2 Å)
主引用文献High-resolution structure of a mutagenic lesion in DNA.
Proc.Natl.Acad.Sci.USA, 87, 1990
2RLN
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BU of 2rln by Molmil
THERMODYNAMIC AND STRUCTURAL CONSEQUENCES OF CHANGING A SULPHUR ATOM TO A METHYLENE GROUP IN THE M13NLE MUTATION IN RIBONUCLEASE S
分子名称: RIBONUCLEASE, RIBONUCLEASE S (S-PROTEIN), SULFATE ION
著者Ratnaparkhi, G, Varadarajan, R.
登録日1994-07-11
公開日1994-11-01
最終更新日2017-11-29
実験手法X-RAY DIFFRACTION (1.85 Å)
主引用文献Thermodynamic and structural consequences of changing a sulfur atom to a methylene group in the M13Nle mutation in ribonuclease-S.
Biochemistry, 33, 1994
3IKD
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BU of 3ikd by Molmil
Structure-Based Design of Novel PIN1 Inhibitors (I)
分子名称: (2R)-2-[(1-benzothiophen-2-ylcarbonyl)amino]-3-phenylpropyl phosphate, Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1
著者Matthews, D, Greasley, S, Ferre, R, Parge, H.
登録日2009-08-05
公開日2009-09-22
最終更新日2024-02-21
実験手法X-RAY DIFFRACTION (2 Å)
主引用文献Structure-based design of novel human Pin1 inhibitors (I).
Bioorg.Med.Chem.Lett., 19, 2009
3IK8
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BU of 3ik8 by Molmil
Structure-Based Design of Novel PIN1 Inhibitors (I)
分子名称: Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1
著者Matthews, D, Greasley, S, Ferre, R.A, Parge, H.
登録日2009-08-05
公開日2009-09-22
最終更新日2024-02-21
実験手法X-RAY DIFFRACTION (1.85 Å)
主引用文献Structure-based design of novel human Pin1 inhibitors (I).
Bioorg.Med.Chem.Lett., 19, 2009
3IKG
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BU of 3ikg by Molmil
Structure-Based Design of Novel PIN1 Inhibitors (I)
分子名称: (2R)-2-[(1-benzothiophen-2-ylcarbonyl)amino]-3-(3-methylphenyl)propyl phosphate, Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1
著者Parge, H, Ferre, R.A, Greasley, S, Matthews, D.
登録日2009-08-05
公開日2009-09-22
最終更新日2023-09-06
実験手法X-RAY DIFFRACTION (1.86 Å)
主引用文献Structure-based design of novel human Pin1 inhibitors (I).
Bioorg.Med.Chem.Lett., 19, 2009
3I6C
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BU of 3i6c by Molmil
Structure-Based Design of Novel PIN1 Inhibitors (II)
分子名称: 3-fluoro-N-(naphthalen-2-ylcarbonyl)-D-phenylalanine, Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1
著者Greasley, S.E, Ferre, R.A.
登録日2009-07-06
公開日2010-04-21
最終更新日2024-02-21
実験手法X-RAY DIFFRACTION (1.3 Å)
主引用文献Structure-based design of novel human Pin1 inhibitors (II).
Bioorg.Med.Chem.Lett., 20, 2010
3JYJ
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BU of 3jyj by Molmil
Structure-Based Design of Novel PIN1 Inhibitors (II)
分子名称: (2R,4E)-2-[(naphthalen-2-ylcarbonyl)amino]-5-phenylpent-4-enoic acid, Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1
著者Greasley, S.E, Ferre, R.A.
登録日2009-09-21
公開日2010-04-07
最終更新日2024-04-03
実験手法X-RAY DIFFRACTION (1.87 Å)
主引用文献Structure-based design of novel human Pin1 inhibitors (II).
Bioorg.Med.Chem.Lett., 20, 2010
1D5D
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BU of 1d5d by Molmil
The role of phenylalanine 8 in the stabilization of the s protein-s peptide interaction: packing and cavities
分子名称: RNASE S, S PEPTIDE, SULFATE ION
著者Ratnaparkhi, G.S, Varadarajan, R.
登録日1999-10-07
公開日1999-10-20
最終更新日2018-03-14
実験手法X-RAY DIFFRACTION (2.25 Å)
主引用文献Thermodynamic and structural studies of cavity formation in proteins suggest that loss of packing interactions rather than the hydrophobic effect dominates the observed energetics.
Biochemistry, 39, 2000
1D5E
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BU of 1d5e by Molmil
The role of phenylalanine 8 in the stabilization of the S protein-S peptide interaction: Packing and cavities
分子名称: RNASE S, S PEPTIDE, SULFATE ION
著者Ratnaparkhi, G.S, Varadarajan, R.
登録日1999-10-07
公開日1999-10-20
最終更新日2023-11-15
実験手法X-RAY DIFFRACTION (2.25 Å)
主引用文献Thermodynamic and structural studies of cavity formation in proteins suggest that loss of packing interactions rather than the hydrophobic effect dominates the observed energetics.
Biochemistry, 39, 2000
1D5H
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BU of 1d5h by Molmil
Rnase s(f8a). mutant ribonucleasE S.
分子名称: RNASE S, S PEPTIDE, SULFATE ION
著者Ratnaparkhi, G.S, Varadarajan, R.
登録日1999-10-07
公開日1999-10-20
最終更新日2018-03-14
実験手法X-RAY DIFFRACTION (2.25 Å)
主引用文献Thermodynamic and structural studies of cavity formation in proteins suggest that loss of packing interactions rather than the hydrophobic effect dominates the observed energetics.
Biochemistry, 39, 2000

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件を2024-04-24に公開中

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