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Magnesium in PDB 1bg0: Transition State Structure of Arginine Kinase

Enzymatic activity of Transition State Structure of Arginine Kinase

All present enzymatic activity of Transition State Structure of Arginine Kinase:
2.7.3.3;

Protein crystallography data

The structure of Transition State Structure of Arginine Kinase, PDB code: 1bg0 was solved by G.Zhou, T.Somasundaram, E.Blanc, G.Parthasarathy, 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) 5.00 / 1.86
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 65.439, 70.885, 80.437, 90.00, 90.00, 90.00
R / Rfree (%) 19.6 / 22.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Transition State Structure of Arginine Kinase (pdb code 1bg0). 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 Transition State Structure of Arginine Kinase, PDB code: 1bg0:

Magnesium binding site 1 out of 1 in 1bg0

Go back to Magnesium Binding Sites List in 1bg0
Magnesium binding site 1 out of 1 in the Transition State Structure of Arginine Kinase


Mono view


Stereo pair view

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

b:8.8
occ:1.00
O A:HOH796 2.0 5.5 1.0
O1B A:ADP400 2.1 11.0 1.0
O A:HOH798 2.1 9.8 1.0
O1A A:ADP400 2.1 8.2 1.0
O A:HOH797 2.2 7.2 1.0
O1 A:NO3401 2.2 10.8 1.0
N A:NO3401 3.2 8.2 1.0
PB A:ADP400 3.3 9.2 1.0
PA A:ADP400 3.3 8.6 1.0
O3 A:NO3401 3.5 10.3 1.0
O3A A:ADP400 3.5 9.2 1.0
O A:HOH715 3.9 7.4 1.0
O3B A:ADP400 4.0 9.0 1.0
OE2 A:GLU314 4.2 12.0 1.0
NH1 A:ARG229 4.2 7.5 1.0
OE2 A:GLU224 4.2 9.2 1.0
CZ3 A:TRP221 4.2 7.6 1.0
O A:HOH723 4.2 12.1 1.0
NH2 A:DAR403 4.3 6.0 1.0
O2A A:ADP400 4.3 8.7 1.0
O5' A:ADP400 4.4 7.8 1.0
O2B A:ADP400 4.4 10.4 1.0
C5' A:ADP400 4.4 8.0 1.0
OE1 A:GLU225 4.4 8.1 1.0
OE1 A:GLU224 4.4 7.6 1.0
O A:HOH714 4.5 12.9 1.0
O2 A:NO3401 4.5 11.9 1.0
CH2 A:TRP221 4.5 8.6 1.0
CD A:GLU224 4.8 7.3 1.0
CD A:GLU314 4.8 11.9 1.0
NH1 A:ARG309 5.0 7.7 1.0

Reference:

G.Zhou, T.Somasundaram, E.Blanc, G.Parthasarathy, W.R.Ellington, M.S.Chapman. Transition State Structure of Arginine Kinase: Implications For Catalysis of Bimolecular Reactions. Proc.Natl.Acad.Sci.Usa V. 95 8449 1998.
ISSN: ISSN 0027-8424
PubMed: 9671698
DOI: 10.1073/PNAS.95.15.8449
Page generated: Tue Aug 13 02:12:53 2024

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