Magnesium in PDB 5a9f: Crystal Structure of the Helicase Domain of Human Dna Polymerase Theta in Complex with Adp

Enzymatic activity of Crystal Structure of the Helicase Domain of Human Dna Polymerase Theta in Complex with Adp

All present enzymatic activity of Crystal Structure of the Helicase Domain of Human Dna Polymerase Theta in Complex with Adp:
2.7.7.7;

Protein crystallography data

The structure of Crystal Structure of the Helicase Domain of Human Dna Polymerase Theta in Complex with Adp, PDB code: 5a9f was solved by J.A.Newman, C.D.O.Cooper, H.Aitkenhead, D.M.Pinkas, K.Kupinska, N.Burgess-Brown, F.Von Delft, C.H.Arrowsmith, A.Edwards, C.Bountra, O.Gileadi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.111 / 3.20
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 115.767, 133.740, 162.697, 90.00, 90.00, 90.00
R / Rfree (%) 22.63 / 27.31

Other elements in 5a9f:

The structure of Crystal Structure of the Helicase Domain of Human Dna Polymerase Theta in Complex with Adp also contains other interesting chemical elements:

Potassium (K) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Helicase Domain of Human Dna Polymerase Theta in Complex with Adp (pdb code 5a9f). 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 the Helicase Domain of Human Dna Polymerase Theta in Complex with Adp, PDB code: 5a9f:

Magnesium binding site 1 out of 1 in 5a9f

Go back to Magnesium Binding Sites List in 5a9f
Magnesium binding site 1 out of 1 in the Crystal Structure of the Helicase Domain of Human Dna Polymerase Theta in Complex with Adp


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 the Helicase Domain of Human Dna Polymerase Theta in Complex with Adp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1894

b:91.5
occ:1.00
OD1 A:ASP216 3.6 0.4 1.0
O3B A:ADP1892 3.8 0.3 1.0
OD2 A:ASP216 4.1 0.1 1.0
CE A:LYS121 4.1 0.2 1.0
OE2 A:GLU217 4.1 0.7 1.0
OE1 A:GLU217 4.2 1.0 1.0
CD A:GLU217 4.2 0.9 1.0
CG A:ASP216 4.3 0.5 1.0
O1B A:ADP1892 4.3 0.3 1.0
PB A:ADP1892 4.3 0.8 1.0
NZ A:LYS121 4.4 0.5 1.0
O2B A:ADP1892 4.5 0.4 1.0

Reference:

J.A.Newman, C.D.O.Cooper, H.Aitkenhead, O.Gileadi. Structure of the Helicase Domain of Dna Polymerase Theta Reveals A Possible Role in the Microhomology-Mediated End- Joining Pathway. Structure V. 23 2319 2015.
ISSN: ISSN 0969-2126
PubMed: 26636256
DOI: 10.1016/J.STR.2015.10.014
Page generated: Mon Dec 14 19:59:58 2020

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