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Magnesium in PDB 1p52: Structure of Arginine Kinase E314D Mutant

Enzymatic activity of Structure of Arginine Kinase E314D Mutant

All present enzymatic activity of Structure of Arginine Kinase E314D Mutant:
2.7.3.3;

Protein crystallography data

The structure of Structure of Arginine Kinase E314D Mutant, PDB code: 1p52 was solved by P.S.Pruett, A.Azzi, S.A.Clark, M.S.Yousef, J.L.Gattis, T.Somasundarum, W.R.Ellington, M.S.Chapman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 65.393, 70.312, 80.139, 90.00, 90.00, 90.00
R / Rfree (%) 17.8 / 23.5

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Arginine Kinase E314D Mutant (pdb code 1p52). 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 Arginine Kinase E314D Mutant, PDB code: 1p52:

Magnesium binding site 1 out of 1 in 1p52

Go back to Magnesium Binding Sites List in 1p52
Magnesium binding site 1 out of 1 in the Structure of Arginine Kinase E314D Mutant


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Arginine Kinase E314D Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg402

b:17.0
occ:1.00
O1B A:ADP400 2.0 15.2 1.0
O1A A:ADP400 2.0 13.4 1.0
O A:HOH892 2.1 17.0 1.0
O1 A:NO3401 2.1 19.7 1.0
O A:HOH893 2.1 17.1 1.0
O A:HOH891 2.2 13.6 1.0
PB A:ADP400 3.2 16.9 1.0
PA A:ADP400 3.2 19.3 1.0
N A:NO3401 3.3 29.8 1.0
O3A A:ADP400 3.5 19.2 1.0
O3 A:NO3401 3.6 26.9 1.0
O A:HOH516 3.8 16.3 1.0
O3B A:ADP400 4.0 16.9 1.0
NH2 A:DAR403 4.2 23.6 1.0
NH1 A:ARG229 4.2 18.5 1.0
OE2 A:GLU224 4.2 15.3 1.0
CZ3 A:TRP221 4.3 14.8 1.0
O5' A:ADP400 4.3 17.4 1.0
O2B A:ADP400 4.3 17.7 1.0
O2A A:ADP400 4.3 19.4 1.0
O A:HOH596 4.3 29.2 1.0
C5' A:ADP400 4.4 17.3 1.0
OE2 A:GLU225 4.4 15.1 1.0
OE1 A:GLU224 4.5 12.6 1.0
O A:HOH507 4.6 14.7 1.0
CH2 A:TRP221 4.6 21.7 1.0
O2 A:NO3401 4.6 17.8 1.0
OD2 A:ASP314 4.8 31.1 1.0
CD A:GLU224 4.8 20.4 1.0
NH1 A:ARG309 4.9 22.4 1.0

Reference:

P.S.Pruett, A.Azzi, S.A.Clark, M.S.Yousef, J.L.Gattis, T.Somasundaram, W.R.Ellington, M.S.Chapman. The Putative Catalytic Bases Have, at Most, An Accessory Role in the Mechanism of Arginine Kinase. J.Biol.Chem. V. 278 26952 2003.
ISSN: ISSN 0021-9258
PubMed: 12732621
DOI: 10.1074/JBC.M212931200
Page generated: Tue Aug 13 10:48:59 2024

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