Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help
Search by PDB author
6QXZ
DownloadVisualize
BU of 6qxz by Molmil
Solution structure of the ASHH2 CW domain with the N-terminal histone H3 tail mimicking peptide monomethylated on lysine 4
Descriptor: ALA-ARG-THR-MLZ-GLN-THR-ALA-ARG-TYR, Histone-lysine N-methyltransferase ASHH2, ZINC ION
Authors:Dobrovolska, O, Madeleine, N, Teigen, K, Halskau, O, Bril'kov, M.
Deposit date:2019-03-08
Release date:2019-12-04
Last modified:2023-06-14
Method:SOLUTION NMR
Cite:The Arabidopsis (ASHH2) CW domain binds monomethylated K4 of the histone H3 tail through conformational selection.
Febs J., 287, 2020
7PIM
DownloadVisualize
BU of 7pim by Molmil
Partial structure of tyrosine hydroxylase lacking the first 35 residues in complex with dopamine.
Descriptor: FE (III) ION, L-DOPAMINE, Regulatory domain alpha-helix, ...
Authors:Bueno-Carrasco, M.T, Cuellar, J, Santiago, C, Valpuesta, J.M, Martinez, A, Flydal, M.I.
Deposit date:2021-08-20
Release date:2021-12-22
Last modified:2024-07-17
Method:ELECTRON MICROSCOPY (4.6 Å)
Cite:Structural mechanism for tyrosine hydroxylase inhibition by dopamine and reactivation by Ser40 phosphorylation.
Nat Commun, 13, 2022
4J6S
DownloadVisualize
BU of 4j6s by Molmil
14-3-3gamma complexed with the N-terminal sequence of tyrosine hydroxylase (residues 1-43)
Descriptor: 14-3-3 protein gamma, N-terminal motif of tyrosine hydroxylase
Authors:Mileni, M, Martinez, A, Stevens, R.C.
Deposit date:2013-02-11
Release date:2013-10-02
Last modified:2023-09-20
Method:X-RAY DIFFRACTION (3.08 Å)
Cite:The N-terminal sequence of tyrosine hydroxylase is a conformationally versatile motif that binds 14-3-3 proteins and membranes.
J.Mol.Biol., 426, 2014
6ZVP
DownloadVisualize
BU of 6zvp by Molmil
Atomic model of the EM-based structure of the full-length tyrosine hydroxylase in complex with dopamine (residues 40-497) in which the regulatory domain (residues 40-165) has been included only with the backbone atoms
Descriptor: FE (III) ION, L-DOPAMINE, Tyrosine 3-monooxygenase
Authors:Bueno-Carrasco, M.T, Cuellar, J, Santiago, C, Valpuesta, J.M, Martinez, A, Flydal, M.I.
Deposit date:2020-07-27
Release date:2021-11-17
Last modified:2022-02-02
Method:ELECTRON MICROSCOPY (4 Å)
Cite:Structural mechanism for tyrosine hydroxylase inhibition by dopamine and reactivation by Ser40 phosphorylation.
Nat Commun, 13, 2022
6ZZU
DownloadVisualize
BU of 6zzu by Molmil
Partial structure of the substrate-free tyrosine hydroxylase (apo-TH).
Descriptor: FE (III) ION, Tyrosine 3-monooxygenase
Authors:Bueno-Carrasco, M.T, Cuellar, J, Santiago, C, Valpuesta, J.M, Martinez, A, Flydal, M.I.
Deposit date:2020-08-05
Release date:2021-11-17
Last modified:2024-07-10
Method:ELECTRON MICROSCOPY (3.5 Å)
Cite:Structural mechanism for tyrosine hydroxylase inhibition by dopamine and reactivation by Ser40 phosphorylation.
Nat Commun, 13, 2022
7A2G
DownloadVisualize
BU of 7a2g by Molmil
Full-length structure of the substrate-free tyrosine hydroxylase (apo-TH).
Descriptor: FE (III) ION, Tyrosine 3-monooxygenase
Authors:Bueno-Carrasco, M.T, Cuellar, J, Santiago, C, Flydal, M.I, Martinez, A, Valpuesta, J.M.
Deposit date:2020-08-17
Release date:2021-12-01
Last modified:2024-07-10
Method:ELECTRON MICROSCOPY (4.1 Å)
Cite:Structural mechanism for tyrosine hydroxylase inhibition by dopamine and reactivation by Ser40 phosphorylation.
Nat Commun, 13, 2022
6ZN2
DownloadVisualize
BU of 6zn2 by Molmil
Partial structure of tyrosine hydroxylase in complex with dopamine showing the catalytic domain and an alpha-helix from the regulatory domain involved in dopamine binding.
Descriptor: FE (III) ION, L-DOPAMINE, SER-LEU-ILE-GLU-ASP-ALA-ARG-LYS-GLU-ARG-GLU-ALA-ALA-VAL-ALA-ALA-ALA-ALA, ...
Authors:Bueno-Carrasco, M.T, Cuellar, J, Santiago, C, Valpuesta, J.M, Martinez, A, Flydal, M.I.
Deposit date:2020-07-06
Release date:2021-12-08
Last modified:2024-07-10
Method:ELECTRON MICROSCOPY (4.3 Å)
Cite:Structural mechanism for tyrosine hydroxylase inhibition by dopamine and reactivation by Ser40 phosphorylation.
Nat Commun, 13, 2022

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon