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Magnesium in PDB 4p3d: MT1-Mmp:Fab Complex (Form II)

Enzymatic activity of MT1-Mmp:Fab Complex (Form II)

All present enzymatic activity of MT1-Mmp:Fab Complex (Form II):
3.4.24.80;

Protein crystallography data

The structure of MT1-Mmp:Fab Complex (Form II), PDB code: 4p3d was solved by H.Rozenberg, Y.Udi, I.Sagi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.66 / 1.95
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 52.898, 96.226, 81.521, 90.00, 92.36, 90.00
R / Rfree (%) 15.8 / 21

Other elements in 4p3d:

The structure of MT1-Mmp:Fab Complex (Form II) also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the MT1-Mmp:Fab Complex (Form II) (pdb code 4p3d). 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 MT1-Mmp:Fab Complex (Form II), PDB code: 4p3d:

Magnesium binding site 1 out of 1 in 4p3d

Go back to Magnesium Binding Sites List in 4p3d
Magnesium binding site 1 out of 1 in the MT1-Mmp:Fab Complex (Form II)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of MT1-Mmp:Fab Complex (Form II) within 5.0Å range:
probe atom residue distance (Å) B Occ
L:Mg301

b:12.3
occ:0.56
O L:HOH412 1.9 16.0 0.7
O L:HOH419 1.9 22.7 1.0
O L:HOH448 2.0 23.4 1.0
O L:HOH430 2.2 15.0 1.0
O L:HOH436 2.4 13.2 1.0
OG1 L:THR77 3.7 8.1 1.0
OD1 L:ASP75 3.9 9.8 0.5
OD2 L:ASP75 3.9 12.2 0.5
OG L:SER22 4.1 14.2 1.0
O L:HOH453 4.1 28.7 0.7
O L:HOH536 4.1 28.6 1.0
O L:HOH493 4.1 18.4 1.0
O L:HOH569 4.2 12.9 1.0
CG L:ASP75 4.3 11.3 0.5
CB L:SER22 4.9 10.4 1.0

Reference:

Y.Udi, M.Grossman, I.Solomonov, O.Dym, H.Rozenberg, V.Moreno, P.Cuniasse, V.Dive, A.G.Arroyo, I.Sagi. Inhibition Mechanism of Membrane Metalloprotease By An Exosite-Swiveling Conformational Antibody. Structure 2014.
ISSN: ISSN 0969-2126
PubMed: 25482542
DOI: 10.1016/J.STR.2014.10.012
Page generated: Mon Dec 14 19:19:08 2020

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