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Magnesium in PDB 1ai3: Orbital Steering in the Catalytic Power of Enzymes: Small Structural Changes with Large Catalytic Consequences

Enzymatic activity of Orbital Steering in the Catalytic Power of Enzymes: Small Structural Changes with Large Catalytic Consequences

All present enzymatic activity of Orbital Steering in the Catalytic Power of Enzymes: Small Structural Changes with Large Catalytic Consequences:
1.1.1.42;

Protein crystallography data

The structure of Orbital Steering in the Catalytic Power of Enzymes: Small Structural Changes with Large Catalytic Consequences, PDB code: 1ai3 was solved by B.L.Stoddard, A.Mesecar, D.E.Koshland Junior, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.90
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 102.400, 102.400, 150.700, 90.00, 90.00, 90.00
R / Rfree (%) 18.8 / 22

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Orbital Steering in the Catalytic Power of Enzymes: Small Structural Changes with Large Catalytic Consequences (pdb code 1ai3). 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 Orbital Steering in the Catalytic Power of Enzymes: Small Structural Changes with Large Catalytic Consequences, PDB code: 1ai3:

Magnesium binding site 1 out of 1 in 1ai3

Go back to Magnesium Binding Sites List in 1ai3
Magnesium binding site 1 out of 1 in the Orbital Steering in the Catalytic Power of Enzymes: Small Structural Changes with Large Catalytic Consequences


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Orbital Steering in the Catalytic Power of Enzymes: Small Structural Changes with Large Catalytic Consequences within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg419

b:30.2
occ:1.00
O A:HOH459 2.0 43.5 1.0
O A:HOH458 2.0 35.8 1.0
O7 A:ICT418 2.1 45.6 0.0
O2 A:ICT418 2.4 43.8 0.0
OD1 A:ASP307 2.4 15.2 1.0
OD1 A:ASP311 3.0 18.4 1.0
C2 A:ICT418 3.0 42.6 0.0
CG A:ASP307 3.1 14.2 1.0
C1 A:ICT418 3.1 47.9 0.0
OD2 A:ASP307 3.3 14.3 1.0
CG A:ASP311 4.0 20.1 1.0
O A:ASP307 4.2 11.4 1.0
NH2 A:ARG129 4.2 23.3 1.0
C3 A:ICT418 4.3 51.6 0.0
CB A:ASP307 4.3 11.4 1.0
O1 A:ICT418 4.3 46.5 0.0
C6 A:ICT418 4.4 40.1 0.0
CA A:ASP307 4.4 11.6 1.0
NH1 A:ARG153 4.4 10.4 1.0
OD2 A:ASP311 4.4 21.0 1.0
O A:HOH596 4.5 22.8 1.0
NH1 A:ARG129 4.5 30.0 1.0
C A:ASP307 4.6 10.7 1.0
OH A:TYR160 4.7 20.2 1.0
O5 A:ICT418 4.7 39.6 0.0
O6 A:ICT418 4.8 36.9 0.0
CZ A:ARG129 4.9 29.6 1.0

Reference:

A.D.Mesecar, B.L.Stoddard, D.E.Koshland Jr.. Orbital Steering in the Catalytic Power of Enzymes: Small Structural Changes with Large Catalytic Consequences. Science V. 277 202 1997.
ISSN: ISSN 0036-8075
PubMed: 9211842
DOI: 10.1126/SCIENCE.277.5323.202
Page generated: Mon Dec 14 03:31:43 2020

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