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2B5S
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BU of 2b5s by Molmil
Crystal structure of peach Pru p3, the prototypic member of the family of plant non-specific lipid transfer protein pan-allergens
Descriptor: HEPTANE, LAURIC ACID, Non-specific lipid transfer protein, ...
Authors:Pasquato, N, Berni, R, Folli, C, Folloni, S, Cianci, M, Pantano, S, Helliwell, R.J, Zanotti, G.
Deposit date:2005-09-29
Release date:2005-11-29
Last modified:2023-08-23
Method:X-RAY DIFFRACTION (2.35 Å)
Cite:Crystal Structure of Peach Pru p 3, the Prototypic Member of the Family of Plant Non-specific Lipid Transfer Protein Pan-allergens
J.Mol.Biol., 356, 2006
2ALG
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BU of 2alg by Molmil
Crystal structure of peach Pru p3, the prototypic member of the family of plant non-specific lipid transfer protein pan-allergens
Descriptor: HEPTANE, HEXAETHYLENE GLYCOL, LAURIC ACID, ...
Authors:Pasquato, N, Berni, R, Folli, C, Folloni, S, Cianci, M, Pantano, S, Helliwell, J, Zanotti, G.
Deposit date:2005-08-05
Release date:2005-11-29
Last modified:2023-08-23
Method:X-RAY DIFFRACTION (2.3 Å)
Cite:Crystal Structure of Peach Pru p 3, the Prototypic Member of the Family of Plant Non-specific Lipid Transfer Protein Pan-allergens
J.Mol.Biol., 356, 2006
2RDO
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BU of 2rdo by Molmil
50S subunit with EF-G(GDPNP) and RRF bound
Descriptor: 23S RIBOSOMAL RNA, 50S ribosomal protein L1, 50S ribosomal protein L11, ...
Authors:Gao, N, Zavialov, A.V, Ehrenberg, M, Frank, J.
Deposit date:2007-09-24
Release date:2008-03-04
Last modified:2024-02-21
Method:ELECTRON MICROSCOPY (9.1 Å)
Cite:Specific interaction between EF-G and RRF and its implication for GTP-dependent ribosome splitting into subunits.
J.Mol.Biol., 374, 2007
1JTB
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BU of 1jtb by Molmil
LIPID TRANSFER PROTEIN COMPLEXED WITH PALMITOYL COENZYME A, NMR, 16 STRUCTURES
Descriptor: COENZYME A, LIPID TRANSFER PROTEIN, PALMITIC ACID
Authors:Lerche, M.H, Kragelund, B.B, Bech, L.M, Poulsen, F.M.
Deposit date:1996-12-03
Release date:1997-07-07
Last modified:2011-10-05
Method:SOLUTION NMR
Cite:Barley lipid-transfer protein complexed with palmitoyl CoA: the structure reveals a hydrophobic binding site that can expand to fit both large and small lipid-like ligands.
Structure, 5, 1997
1OB0
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BU of 1ob0 by Molmil
Kinetic stabilization of Bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface
Descriptor: ALPHA-AMYLASE, CALCIUM ION, SODIUM ION
Authors:Machius, M, Declerck, N, Huber, R, Wiegand, G.
Deposit date:2003-01-21
Release date:2003-01-30
Last modified:2023-12-13
Method:X-RAY DIFFRACTION (1.83 Å)
Cite:Kinetic Stabilization of Bacillus Licheniformis Alpha-Amylase Through Introduction of Hydrophobic Residues at the Surface
J.Biol.Chem., 278, 2003

219869

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