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Magnesium in PDB 4cf7: Crystal Structure of Adenylate Kinase From Aquifex Aeolicus with Mgadp Bound

Enzymatic activity of Crystal Structure of Adenylate Kinase From Aquifex Aeolicus with Mgadp Bound

All present enzymatic activity of Crystal Structure of Adenylate Kinase From Aquifex Aeolicus with Mgadp Bound:
2.7.4.3;

Protein crystallography data

The structure of Crystal Structure of Adenylate Kinase From Aquifex Aeolicus with Mgadp Bound, PDB code: 4cf7 was solved by S.J.Kerns, R.V.Agafonov, Y.-J.Cho, F.Pontiggia, R.Otten, D.V.Pachov, S.Kutter, L.A.Phung, P.N.Murphy, V.Thai, M.F.Hagan, D.Kern, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.265 / 1.59
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 64.088, 64.697, 86.256, 90.00, 90.00, 90.00
R / Rfree (%) 18.17 / 21.58

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Adenylate Kinase From Aquifex Aeolicus with Mgadp Bound (pdb code 4cf7). 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 Adenylate Kinase From Aquifex Aeolicus with Mgadp Bound, PDB code: 4cf7:

Magnesium binding site 1 out of 1 in 4cf7

Go back to Magnesium Binding Sites List in 4cf7
Magnesium binding site 1 out of 1 in the Crystal Structure of Adenylate Kinase From Aquifex Aeolicus with Mgadp Bound


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 Adenylate Kinase From Aquifex Aeolicus with Mgadp Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1207

b:27.9
occ:1.00
O B:HOH2010 2.0 16.4 0.6
O B:HOH2035 2.1 21.6 1.0
O2B B:ADP1205 2.2 20.4 0.7
O B:HOH2104 2.3 25.8 1.0
O B:HOH2083 2.3 18.7 1.0
O1B B:ADP1204 2.4 14.1 1.0
O B:HOH2010 3.0 18.6 0.4
PB B:ADP1204 3.5 14.5 1.0
O3B B:ADP1204 3.5 15.0 1.0
PB B:ADP1205 3.6 22.1 0.7
O3B B:ADP1205 3.9 24.6 0.7
O2A B:ADP1204 4.0 16.8 1.0
O2A B:ADP1205 4.1 14.6 0.7
O2P B:AMP1206 4.1 14.9 0.3
NH1 B:ARG124 4.1 19.2 1.0
O B:HOH2019 4.2 30.8 1.0
O B:HOH2045 4.3 32.3 1.0
N B:GLY14 4.3 13.8 1.0
O3P B:AMP1206 4.3 16.2 0.3
O1A B:ADP1205 4.4 15.0 0.7
O1P B:AMP1206 4.4 16.6 0.3
CA B:GLY14 4.4 15.0 1.0
P B:AMP1206 4.4 12.5 0.3
O3A B:ADP1205 4.4 21.2 0.7
NH1 B:ARG150 4.4 22.7 1.0
PA B:ADP1205 4.4 15.5 0.7
O3A B:ADP1204 4.4 16.0 1.0
OD2 B:ASP81 4.5 13.9 1.0
O2B B:ADP1204 4.6 13.5 1.0
OD1 B:ASP81 4.6 16.8 1.0
PA B:ADP1204 4.6 15.3 1.0
O1B B:ADP1205 4.7 19.5 0.7
O B:HOH2036 4.8 16.5 1.0
O1A B:ADP1204 5.0 16.4 1.0
CG B:ASP81 5.0 14.8 1.0
NH2 B:ARG36 5.0 22.3 1.0

Reference:

S.J.Kerns, R.V.Agafonov, Y.-J.Cho, F.Pontiggia, R.Otten, D.V.Pachov, S.Kutter, L.A.Phung, P.N.Murphy, V.Thai, M.F.Hagan, D.Kern. Catalytic Strategies Used By Kinases in Phosphoryl- Transfer Reactions To Be Published.
Page generated: Thu Aug 15 16:47:04 2024

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