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Magnesium in PDB 4j5i: Crystal Structure of An Alpha-Ketoglutarate-Dependent Taurine Dioxygenase From Mycobacterium Smegmatis

Enzymatic activity of Crystal Structure of An Alpha-Ketoglutarate-Dependent Taurine Dioxygenase From Mycobacterium Smegmatis

All present enzymatic activity of Crystal Structure of An Alpha-Ketoglutarate-Dependent Taurine Dioxygenase From Mycobacterium Smegmatis:
1.14.11.17;

Protein crystallography data

The structure of Crystal Structure of An Alpha-Ketoglutarate-Dependent Taurine Dioxygenase From Mycobacterium Smegmatis, PDB code: 4j5i 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) 49.40 / 2.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 77.010, 166.680, 99.720, 90.00, 90.57, 90.00
R / Rfree (%) 21.1 / 23.4

Other elements in 4j5i:

The structure of Crystal Structure of An Alpha-Ketoglutarate-Dependent Taurine Dioxygenase From Mycobacterium Smegmatis also contains other interesting chemical elements:

Iron (Fe) 8 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of An Alpha-Ketoglutarate-Dependent Taurine Dioxygenase From Mycobacterium Smegmatis (pdb code 4j5i). 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 An Alpha-Ketoglutarate-Dependent Taurine Dioxygenase From Mycobacterium Smegmatis, PDB code: 4j5i:

Magnesium binding site 1 out of 1 in 4j5i

Go back to Magnesium Binding Sites List in 4j5i
Magnesium binding site 1 out of 1 in the Crystal Structure of An Alpha-Ketoglutarate-Dependent Taurine Dioxygenase From Mycobacterium Smegmatis


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 An Alpha-Ketoglutarate-Dependent Taurine Dioxygenase From Mycobacterium Smegmatis within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mg402

b:3.4
occ:1.00
 O F:HOH538 1.9 3.6 1.0
O F:GLU62 2.1 21.9 1.0
OE2 F:GLU62 2.1 21.6 1.0
O F:HOH539 2.3 8.8 1.0
O F:GLY65 2.7 21.5 1.0
CD F:GLU62 3.2 21.9 1.0
C F:GLU62 3.2 21.2 1.0
CG F:GLU62 3.5 21.8 1.0
C F:GLY65 3.6 21.0 1.0
CA F:GLU62 3.8 21.0 1.0
CB F:GLU62 4.2 21.2 1.0
OE1 F:GLU62 4.3 22.6 1.0
N F:GLY65 4.3 21.3 1.0
CA F:GLY65 4.4 21.2 1.0
N F:LEU63 4.4 20.8 1.0
N F:THR66 4.5 20.4 1.0
CA F:THR66 4.6 20.6 1.0
CA F:LEU63 4.7 21.1 1.0
OG1 F:THR66 4.8 20.8 1.0
C F:LEU63 4.8 21.2 1.0
CD F:PRO67 5.0 21.5 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 18:55:43 2020

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