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Magnesium in PDB 1e2q: Human Thymidylate Kinase Complexed with TP5A and A Magnesium-Ion

Enzymatic activity of Human Thymidylate Kinase Complexed with TP5A and A Magnesium-Ion

All present enzymatic activity of Human Thymidylate Kinase Complexed with TP5A and A Magnesium-Ion:
2.7.4.9;

Protein crystallography data

The structure of Human Thymidylate Kinase Complexed with TP5A and A Magnesium-Ion, PDB code: 1e2q was solved by N.Ostermann, I.Schlichting, R.Brundiers, M.Konrad, J.Reinstein, T.Veit, R.S.Goody, A.Lavie, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.30 / 1.70
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 101.310, 101.100, 49.300, 90.00, 90.00, 90.00
R / Rfree (%) 19.2 / 23

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Human Thymidylate Kinase Complexed with TP5A and A Magnesium-Ion (pdb code 1e2q). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Human Thymidylate Kinase Complexed with TP5A and A Magnesium-Ion, PDB code: 1e2q:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1e2q

Go back to Magnesium Binding Sites List in 1e2q
Magnesium binding site 1 out of 2 in the Human Thymidylate Kinase Complexed with TP5A and A Magnesium-Ion


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human Thymidylate Kinase Complexed with TP5A and A Magnesium-Ion within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg401

b:24.9
occ:1.00
O3G A:ATP302 2.0 33.7 1.0
O1B A:ATP302 2.1 20.6 1.0
O A:HOH2017 2.1 27.4 1.0
O A:HOH2244 2.1 22.4 1.0
OG A:SER20 2.1 18.9 1.0
O A:HOH2117 2.2 22.4 1.0
CB A:SER20 3.2 16.2 1.0
PG A:ATP302 3.2 41.2 1.0
PB A:ATP302 3.3 21.8 1.0
O3B A:ATP302 3.4 27.9 1.0
O2P A:TMP301 4.0 35.7 1.0
N A:SER20 4.0 15.8 1.0
O A:HOH2118 4.1 29.1 1.0
CA A:SER20 4.1 14.0 1.0
OD2 A:ASP96 4.1 21.3 1.0
O A:HOH2122 4.2 40.6 1.0
O2A A:ATP302 4.2 22.3 1.0
O2G A:ATP302 4.2 42.2 1.0
O1G A:ATP302 4.2 44.2 1.0
O1P A:TMP301 4.2 42.8 1.0
P A:TMP301 4.3 39.3 1.0
O3A A:ATP302 4.3 24.0 1.0
O2B A:ATP302 4.3 22.8 1.0
OD1 A:ASP96 4.3 19.6 1.0
O3P A:TMP301 4.4 36.6 1.0
O A:HOH2024 4.7 40.4 1.0
PA A:ATP302 4.7 22.4 1.0
CG A:ASP96 4.7 15.8 1.0
O A:HOH2241 4.7 51.3 1.0
O A:HOH2116 4.8 30.1 1.0
O A:HOH2234 4.9 53.6 1.0
CB A:LYS19 5.0 19.7 1.0

Magnesium binding site 2 out of 2 in 1e2q

Go back to Magnesium Binding Sites List in 1e2q
Magnesium binding site 2 out of 2 in the Human Thymidylate Kinase Complexed with TP5A and A Magnesium-Ion


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Human Thymidylate Kinase Complexed with TP5A and A Magnesium-Ion within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg402

b:25.1
occ:0.50
O A:HOH2063 2.1 31.3 1.0
O A:HOH2135 2.1 29.0 1.0
O A:HOH2132 2.2 28.2 1.0
OE1 A:GLN119 4.2 18.7 1.0
OD2 A:ASP115 4.3 25.8 1.0
OD1 A:ASP115 4.4 25.8 1.0
CD A:GLN119 4.5 18.2 1.0
NE2 A:GLN119 4.6 21.1 1.0
CG A:ASP115 4.8 24.5 1.0

Reference:

N.Ostermann, I.Schlichting, R.Brundiers, M.Konrad, J.Reinstein, T.Veit, R.S.Goody, A.Lavie. Insights Into the Phosphoryltransfer Mechanism of Human Thymidylate Kinase Gained From Crystal Structures of Enzyme Complexes Along the Reaction Coordinate Structure V. 8 629 2000.
ISSN: ISSN 0969-2126
PubMed: 10873853
DOI: 10.1016/S0969-2126(00)00149-0
Page generated: Tue Aug 13 02:50:49 2024

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