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PDB: 54 results

5OD5
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BU of 5od5 by Molmil
Periplasmic binding protein CeuE complexed with a synthetic catalyst
Descriptor: 2,5,8,11,14,17,20,23-OCTAOXAPENTACOSAN-25-OL, 4-(aminomethyl)-~{N}-(pyridin-2-ylmethyl)benzenesulfonamide, Azotochelin, ...
Authors:Duhme-Klair, A.K, Raines, D.J, Clarke, J.E, Blagova, E.V, Dodson, E.J, Wilson, K.S.
Deposit date:2017-07-04
Release date:2018-08-01
Last modified:2024-05-08
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Redox-switchable siderophore anchor enables reversible artificial metalloenzyme assembly
Nat Catal, 2018
3O9P
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BU of 3o9p by Molmil
The structure of the Escherichia coli murein tripeptide binding protein MppA
Descriptor: L-ALA-GAMMA-D-GLU-MESO-DIAMINOPIMELIC ACID, Periplasmic murein peptide-binding protein, ZINC ION
Authors:Maqbool, A, Levdikov, V.M, Blagova, E.V, Wilkinson, A.J, Thomas, G.H.
Deposit date:2010-08-04
Release date:2011-07-06
Last modified:2023-09-06
Method:X-RAY DIFFRACTION (2.07 Å)
Cite:Compensating Stereochemical Changes Allow Murein Tripeptide to Be Accommodated in a Conventional Peptide-binding Protein.
J.Biol.Chem., 286, 2011
5MQH
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Structure of the Phosphatase Domain of the Cell Fate Determinant SpoIIE from Bacillus subtilis in a crystal form without domain swapping
Descriptor: Serine phosphatase
Authors:Levdikov, V.M, Wilkinson, A.J, Blagova, E.V.
Deposit date:2016-12-20
Release date:2017-05-31
Last modified:2024-01-17
Method:X-RAY DIFFRACTION (2.45 Å)
Cite:A widespread family of serine/threonine protein phosphatases shares a common regulatory switch with proteasomal proteases.
Elife, 6, 2017
3O6Q
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The Structure of SpoIISA and SpoIISB, a Toxin - Antitoxin System
Descriptor: Stage II sporulation protein SA, Stage II sporulation protein SB
Authors:Levdikov, V.M, Blagova, E.V, Lebedev, A.A, Wilkinson, A.J, Florek, P, Barak, I.
Deposit date:2010-07-29
Release date:2010-12-08
Last modified:2024-10-09
Method:X-RAY DIFFRACTION (2.5 Å)
Cite:The structure and interactions of SpoIISA and SpoIISB, a toxin-antitoxin system in Bacillus subtilis.
J.Biol.Chem., 161, 2010
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