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Magnesium in PDB 4dzi: Crystal Structure of Amidohydrolase MAP2389C (Target Efi-500390) From Mycobacterium Avium Subsp. Paratuberculosis K-10

Protein crystallography data

The structure of Crystal Structure of Amidohydrolase MAP2389C (Target Efi-500390) From Mycobacterium Avium Subsp. Paratuberculosis K-10, PDB code: 4dzi was solved by Y.Patskovsky, R.Toro, R.Bhosle, B.Hillerich, R.D.Seidel, E.Washington, A.Scott Glenn, S.Chowdhury, B.Evans, J.Hammonds, W.D.Zencheck, H.J.Imker, J.A.Gerlt, F.M.Raushel, S.C.Almo, Enzyme Function Initiative (Efi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 75.106, 136.131, 93.229, 90.00, 113.09, 90.00
R / Rfree (%) 16.6 / 20.3

Other elements in 4dzi:

The structure of Crystal Structure of Amidohydrolase MAP2389C (Target Efi-500390) From Mycobacterium Avium Subsp. Paratuberculosis K-10 also contains other interesting chemical elements:

Cadmium (Cd) 8 atoms
Chlorine (Cl) 6 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Amidohydrolase MAP2389C (Target Efi-500390) From Mycobacterium Avium Subsp. Paratuberculosis K-10 (pdb code 4dzi). 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 Crystal Structure of Amidohydrolase MAP2389C (Target Efi-500390) From Mycobacterium Avium Subsp. Paratuberculosis K-10, PDB code: 4dzi:

Magnesium binding site 1 out of 1 in 4dzi

Go back to Magnesium Binding Sites List in 4dzi
Magnesium binding site 1 out of 1 in the Crystal Structure of Amidohydrolase MAP2389C (Target Efi-500390) From Mycobacterium Avium Subsp. Paratuberculosis K-10


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Amidohydrolase MAP2389C (Target Efi-500390) From Mycobacterium Avium Subsp. Paratuberculosis K-10 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg504

b:30.1
occ:1.00
O A:HOH649 2.0 21.3 1.0
O A:HOH843 2.0 28.3 1.0
O A:HOH747 2.1 24.7 1.0
O A:HOH928 2.1 31.5 1.0
O A:HOH909 2.1 28.9 1.0
O A:HOH736 2.1 23.9 1.0
O A:ARG325 4.1 17.7 1.0
O A:HOH929 4.1 33.8 1.0
O A:ILE345 4.1 20.0 1.0
OD2 A:ASP348 4.2 35.0 1.0
OD1 A:ASP348 4.3 31.9 1.0
CB A:ARG325 4.4 15.3 1.0
C A:ARG325 4.6 14.4 1.0
O A:HOH800 4.6 27.5 1.0
O A:HOH786 4.6 26.1 1.0
CG A:ASP348 4.7 32.0 1.0
O A:HOH790 4.8 28.2 1.0

Reference:

Y.Patskovsky, R.Toro, R.Bhosle, B.Hillerich, R.D.Seidel, E.Washington, A.Scott Glenn, S.Chowdhury, B.Evans, J.Hammonds, W.D.Zencheck, H.J.Imker, J.A.Gerlt, F.M.Raushel, S.C.Almo. Crystal Structure of Amidohydrolase MAP2389C (Target Efi-500390) From Mycobacterium Avium To Be Published.
Page generated: Mon Dec 14 13:25:14 2020

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