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Magnesium in PDB 3hpo: Crystal Structure of Fragment Dna Polymerase I From Bacillus Stearothermophilus Y714S Mutant Bound to G:T Mismatch

Enzymatic activity of Crystal Structure of Fragment Dna Polymerase I From Bacillus Stearothermophilus Y714S Mutant Bound to G:T Mismatch

All present enzymatic activity of Crystal Structure of Fragment Dna Polymerase I From Bacillus Stearothermophilus Y714S Mutant Bound to G:T Mismatch:
2.7.7.7;

Protein crystallography data

The structure of Crystal Structure of Fragment Dna Polymerase I From Bacillus Stearothermophilus Y714S Mutant Bound to G:T Mismatch, PDB code: 3hpo was solved by E.Y.Wu, L.S.Beese, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.98 / 1.75
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 90.210, 93.730, 105.510, 90.00, 90.00, 90.00
R / Rfree (%) 20.1 / 24.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Fragment Dna Polymerase I From Bacillus Stearothermophilus Y714S Mutant Bound to G:T Mismatch (pdb code 3hpo). 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 Fragment Dna Polymerase I From Bacillus Stearothermophilus Y714S Mutant Bound to G:T Mismatch, PDB code: 3hpo:

Magnesium binding site 1 out of 1 in 3hpo

Go back to Magnesium Binding Sites List in 3hpo
Magnesium binding site 1 out of 1 in the Crystal Structure of Fragment Dna Polymerase I From Bacillus Stearothermophilus Y714S Mutant Bound to G:T Mismatch


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 Fragment Dna Polymerase I From Bacillus Stearothermophilus Y714S Mutant Bound to G:T Mismatch within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg200

b:18.1
occ:0.80
 O2G A:TTP201 2.0 16.4 0.8
O2A A:TTP201 2.0 17.9 0.8
O A:HOH83 2.0 23.8 1.0
O A:HOH157 2.0 20.3 1.0
O2B A:TTP201 2.2 14.7 0.8
O A:HOH894 2.2 16.9 1.0
PB A:TTP201 3.1 17.6 0.8
PG A:TTP201 3.2 17.9 0.8
PA A:TTP201 3.3 18.5 0.8
O3B A:TTP201 3.6 17.5 0.8
O3A A:TTP201 3.6 17.7 0.8
O3G A:TTP201 3.8 17.6 0.8
O A:HOH889 4.0 21.6 1.0
O1A A:TTP201 4.1 19.6 0.8
O A:HOH42 4.3 17.7 1.0
O5' A:TTP201 4.4 20.1 0.8
O1G A:TTP201 4.4 17.8 0.8
C5' A:TTP201 4.5 18.8 0.8
N A:GLN656 4.5 12.9 0.3
O1B A:TTP201 4.5 16.2 0.8
OD1 A:ASP653 4.6 28.2 1.0
N A:GLN656 4.6 14.2 0.7
O A:HOH78 4.8 23.2 1.0
O A:HOH204 4.8 46.7 1.0
NE2 A:GLN656 4.8 25.1 0.7
CA A:SER655 4.9 14.2 0.3
CA A:SER655 4.9 15.2 0.7

Reference:

E.Y.Wu, L.S.Beese. The Structure of A High Fidelity Dna Polymerase Bound to A Mismatched Nucleotide Reveals An "Ajar" Intermediate Conformation in the Nucleotide Selection Mechanism. J.Biol.Chem. V. 286 19758 2011.
ISSN: ISSN 0021-9258
PubMed: 21454515
DOI: 10.1074/JBC.M110.191130
Page generated: Mon Dec 14 08:14:19 2020

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