Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help
PDB: 3 results

5A6S
DownloadVisualize
BU of 5a6s by Molmil
Crystal structure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product
Descriptor: ENDOLYSIN, GLYCEROL, PENTAETHYLENE GLYCOL, ...
Authors:Dunne, M, Leicht, S, Krichel, B, Mertens, H.D.T, Thompson, A, Krijgsveld, J, Svergun, D.I, GomezTorres, N, Garde, S, Uetrecht, C, Narbad, A, Mayer, M.J, Meijers, R.
Deposit date:2015-07-01
Release date:2015-12-30
Last modified:2024-01-10
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Crystal Structure of the Ctp1L Endolysin Reveals How its Activity is Regulated by a Secondary Translation Product.
J.Biol.Chem., 291, 2016
2WP1
DownloadVisualize
BU of 2wp1 by Molmil
Structure of Brdt bromodomain 2 bound to an acetylated histone H3 peptide
Descriptor: BROMODOMAIN TESTIS-SPECIFIC PROTEIN, HISTONE H3
Authors:Moriniere, J, Rousseaux, S, Steuerwald, U, Soler-Lopez, M, Curtet, S, Vitte, A.-L, Govin, J, Gaucher, J, Sadoul, K, Hart, D.J, Krijgsveld, J, Khochbin, S, Mueller, C.W, Petosa, C.
Deposit date:2009-08-02
Release date:2009-09-22
Last modified:2024-10-23
Method:X-RAY DIFFRACTION (2.1 Å)
Cite:Cooperative Binding of Two Acetylation Marks on a Histone Tail by a Single Bromodomain.
Nature, 461, 2009
2WP2
DownloadVisualize
BU of 2wp2 by Molmil
Structure of Brdt bromodomain BD1 bound to a diacetylated histone H4 peptide.
Descriptor: BROMODOMAIN TESTIS-SPECIFIC PROTEIN, HISTONE H4
Authors:Moriniere, J, Rousseaux, S, Steuerwald, U, Soler-Lopez, M, Curtet, S, Vitte, A.-L, Govin, J, Gaucher, J, Sadoul, K, Hart, D.J, Krijgsveld, J, Khochbin, S, Mueller, C.W, Petosa, C.
Deposit date:2009-08-02
Release date:2009-09-22
Last modified:2024-11-13
Method:X-RAY DIFFRACTION (2.37 Å)
Cite:Cooperative Binding of Two Acetylation Marks on a Histone Tail by a Single Bromodomain.
Nature, 461, 2009

227561

PDB entries from 2024-11-20

PDB statisticsPDBj update infoContact PDBjnumon