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Magnesium in PDB 3r6o: Crystal Structure of A Probable 2-Hydroxyhepta-2,4-Diene-1, 7- Dioateisomerase From Mycobacterium Abscessus

Protein crystallography data

The structure of Crystal Structure of A Probable 2-Hydroxyhepta-2,4-Diene-1, 7- Dioateisomerase From Mycobacterium Abscessus, PDB code: 3r6o was solved by Seattle Structural Genomics Center For Infectious Disease (Ssgcid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.79 / 1.95
Space group I 41
Cell size a, b, c (Å), α, β, γ (°) 90.680, 90.680, 76.130, 90.00, 90.00, 90.00
R / Rfree (%) 15 / 18.5

Other elements in 3r6o:

The structure of Crystal Structure of A Probable 2-Hydroxyhepta-2,4-Diene-1, 7- Dioateisomerase From Mycobacterium Abscessus also contains other interesting chemical elements:

Chlorine (Cl) 3 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of A Probable 2-Hydroxyhepta-2,4-Diene-1, 7- Dioateisomerase From Mycobacterium Abscessus (pdb code 3r6o). 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 A Probable 2-Hydroxyhepta-2,4-Diene-1, 7- Dioateisomerase From Mycobacterium Abscessus, PDB code: 3r6o:

Magnesium binding site 1 out of 1 in 3r6o

Go back to Magnesium Binding Sites List in 3r6o
Magnesium binding site 1 out of 1 in the Crystal Structure of A Probable 2-Hydroxyhepta-2,4-Diene-1, 7- Dioateisomerase From Mycobacterium Abscessus


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 A Probable 2-Hydroxyhepta-2,4-Diene-1, 7- Dioateisomerase From Mycobacterium Abscessus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg400

b:38.4
occ:1.00
OE2 A:GLU139 2.3 18.9 1.0
OD2 A:ASP168 2.6 18.5 1.0
O A:HOH441 2.9 29.1 1.0
O A:LEU88 3.2 21.2 1.0
OE1 A:GLU137 3.2 26.0 1.0
CD A:GLU139 3.2 18.9 1.0
OE1 A:GLU139 3.4 18.8 1.0
CG A:ASP168 3.4 18.3 1.0
CB A:ASP168 3.5 18.3 1.0
CD A:GLU137 3.9 19.7 1.0
C A:LEU88 4.0 21.1 1.0
OE2 A:GLU137 4.1 21.9 1.0
NZ A:LYS193 4.2 19.2 1.0
CB A:ALA87 4.4 19.5 1.0
N A:GLY89 4.6 21.4 1.0
O A:HOH383 4.6 35.0 1.0
CG A:GLU139 4.6 19.1 1.0
OD1 A:ASP168 4.6 18.3 1.0
CA A:GLY89 4.7 22.1 1.0
N A:LEU88 4.7 20.3 1.0
CG2 A:THR263 4.7 20.7 1.0
CB A:GLU137 4.8 19.5 1.0
CA A:GLY262 4.8 20.8 1.0
N A:THR263 4.8 20.9 1.0
CG A:GLU137 4.9 19.8 1.0
O A:HOH341 5.0 27.1 1.0
CA A:ASP168 5.0 18.3 1.0

Reference:

L.Baugh, I.Phan, D.W.Begley, M.C.Clifton, B.Armour, D.M.Dranow, B.M.Taylor, M.M.Muruthi, J.Abendroth, J.W.Fairman, D.Fox, S.H.Dieterich, B.L.Staker, A.S.Gardberg, R.Choi, S.N.Hewitt, A.J.Napuli, J.Myers, L.K.Barrett, Y.Zhang, M.Ferrell, E.Mundt, K.Thompkins, N.Tran, S.Lyons-Abbott, A.Abramov, A.Sekar, D.Serbzhinskiy, D.Lorimer, G.W.Buchko, R.Stacy, L.J.Stewart, T.E.Edwards, W.C.Van Voorhis, P.J.Myler. Increasing the Structural Coverage of Tuberculosis Drug Targets. Tuberculosis (Edinb) V. 95 142 2015.
ISSN: ISSN 1472-9792
PubMed: 25613812
DOI: 10.1016/J.TUBE.2014.12.003
Page generated: Mon Dec 14 08:44:08 2020

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