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Magnesium in PDB 3po5: Structure of A Mutant of the Large Fragment of Dna Polymerase I From Thermus Auqaticus in Complex with An Abasic Site and Ddatp

Enzymatic activity of Structure of A Mutant of the Large Fragment of Dna Polymerase I From Thermus Auqaticus in Complex with An Abasic Site and Ddatp

All present enzymatic activity of Structure of A Mutant of the Large Fragment of Dna Polymerase I From Thermus Auqaticus in Complex with An Abasic Site and Ddatp:
2.7.7.7;

Protein crystallography data

The structure of Structure of A Mutant of the Large Fragment of Dna Polymerase I From Thermus Auqaticus in Complex with An Abasic Site and Ddatp, PDB code: 3po5 was solved by A.Marx, K.Diederichs, S.Obeid, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.33 / 2.39
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 109.301, 109.301, 90.318, 90.00, 90.00, 120.00
R / Rfree (%) 21 / 26.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of A Mutant of the Large Fragment of Dna Polymerase I From Thermus Auqaticus in Complex with An Abasic Site and Ddatp (pdb code 3po5). 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 Structure of A Mutant of the Large Fragment of Dna Polymerase I From Thermus Auqaticus in Complex with An Abasic Site and Ddatp, PDB code: 3po5:

Magnesium binding site 1 out of 1 in 3po5

Go back to Magnesium Binding Sites List in 3po5
Magnesium binding site 1 out of 1 in the Structure of A Mutant of the Large Fragment of Dna Polymerase I From Thermus Auqaticus in Complex with An Abasic Site and Ddatp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of A Mutant of the Large Fragment of Dna Polymerase I From Thermus Auqaticus in Complex with An Abasic Site and Ddatp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1

b:64.3
occ:1.00
 O A:HOH122 2.1 39.7 1.0
O2B A:DDS835 2.4 69.4 1.0
O2A A:DDS835 2.8 96.6 1.0
OD1 A:ASP610 3.2 52.2 1.0
O3G A:DDS835 3.2 77.4 1.0
O A:HOH124 3.5 41.5 1.0
PB A:DDS835 3.7 67.7 1.0
O A:TYR611 3.8 39.2 1.0
PA A:DDS835 3.9 94.8 1.0
CG A:ASP610 4.1 52.4 1.0
CA A:SER612 4.2 48.2 1.0
O5' A:DDS835 4.2 81.7 1.0
O3A A:DDS835 4.3 0.3 1.0
PG A:DDS835 4.3 79.9 1.0
O A:HOH123 4.3 38.7 1.0
O3B A:DDS835 4.3 50.3 1.0
OD2 A:ASP610 4.4 53.0 1.0
OE1 A:GLU820 4.6 64.6 1.0
N A:GLN613 4.7 40.7 1.0
C A:TYR611 4.7 39.9 1.0
OG A:SER612 4.7 50.0 1.0
O A:HOH125 4.8 45.9 1.0
CB A:SER612 4.9 49.6 1.0
O1G A:DDS835 4.9 80.5 1.0
O1B A:DDS835 4.9 59.2 1.0
N A:SER612 4.9 46.6 1.0
OE2 A:GLU820 5.0 65.1 1.0

Reference:

S.Obeid, A.Schnur, C.Gloeckner, N.Blatter, W.Welte, K.Diederichs, A.Marx. Learning From Directed Evolution: Thermus Aquaticus Dna Polymerase Mutants with Translesion Synthesis Activity. Chembiochem V. 12 1574 2011.
ISSN: ISSN 1439-4227
PubMed: 21480455
DOI: 10.1002/CBIC.201000783
Page generated: Mon Dec 14 08:40:35 2020

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