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Magnesium in PDB 5fgj: Structure of Tetrameric Rat Phenylalanine Hydroxylase, Residues 1-453

Enzymatic activity of Structure of Tetrameric Rat Phenylalanine Hydroxylase, Residues 1-453

All present enzymatic activity of Structure of Tetrameric Rat Phenylalanine Hydroxylase, Residues 1-453:
1.14.16.1;

Protein crystallography data

The structure of Structure of Tetrameric Rat Phenylalanine Hydroxylase, Residues 1-453, PDB code: 5fgj was solved by A.B.Taylor, K.M.Roberts, P.F.Fitzpatrick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 101.48 / 3.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 96.768, 102.686, 202.966, 90.00, 90.00, 90.00
R / Rfree (%) 26.8 / 29.6

Other elements in 5fgj:

The structure of Structure of Tetrameric Rat Phenylalanine Hydroxylase, Residues 1-453 also contains other interesting chemical elements:

Iron (Fe) 4 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Tetrameric Rat Phenylalanine Hydroxylase, Residues 1-453 (pdb code 5fgj). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Structure of Tetrameric Rat Phenylalanine Hydroxylase, Residues 1-453, PDB code: 5fgj:

Magnesium binding site 1 out of 1 in 5fgj

Go back to Magnesium Binding Sites List in 5fgj
Magnesium binding site 1 out of 1 in the Structure of Tetrameric Rat Phenylalanine Hydroxylase, Residues 1-453


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Tetrameric Rat Phenylalanine Hydroxylase, Residues 1-453 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg502

b:58.4
occ:1.00
OE2 A:GLU178 2.4 64.0 1.0
CD A:GLU178 3.6 64.0 1.0
OE2 A:GLU181 3.8 68.1 1.0
CG A:GLU178 4.2 64.0 1.0
O A:TYR179 4.3 64.4 1.0
OE1 A:GLU178 4.6 64.0 1.0
CD A:GLU181 4.7 68.1 1.0
CG A:GLU181 4.7 68.1 1.0

Reference:

S.P.Meisburger, A.B.Taylor, C.A.Khan, S.Zhang, P.F.Fitzpatrick, N.Ando. Domain Movements Upon Activation of Phenylalanine Hydroxylase Characterized By Crystallography and Chromatography-Coupled Small-Angle X-Ray Scattering. J.Am.Chem.Soc. V. 138 6506 2016.
ISSN: ESSN 1520-5126
PubMed: 27145334
DOI: 10.1021/JACS.6B01563
Page generated: Tue Aug 12 08:07:20 2025

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