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Magnesium in PDB 4cgp: Leishmania Major N-Myristoyltransferase in Complex with Cofactor

Enzymatic activity of Leishmania Major N-Myristoyltransferase in Complex with Cofactor

All present enzymatic activity of Leishmania Major N-Myristoyltransferase in Complex with Cofactor:
2.3.1.97;

Protein crystallography data

The structure of Leishmania Major N-Myristoyltransferase in Complex with Cofactor, PDB code: 4cgp was solved by J.A.Brannigan, S.M.Roberts, A.S.Bell, J.A.Hutton, D.F.Smith, E.W.Tate, R.J.Leatherbarrow, A.J.Wilkinson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.26 / 1.40
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 47.711, 91.197, 53.019, 90.00, 111.71, 90.00
R / Rfree (%) 15.933 / 19.638

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Leishmania Major N-Myristoyltransferase in Complex with Cofactor (pdb code 4cgp). 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 Leishmania Major N-Myristoyltransferase in Complex with Cofactor, PDB code: 4cgp:

Magnesium binding site 1 out of 1 in 4cgp

Go back to Magnesium Binding Sites List in 4cgp
Magnesium binding site 1 out of 1 in the Leishmania Major N-Myristoyltransferase in Complex with Cofactor


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Leishmania Major N-Myristoyltransferase in Complex with Cofactor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1422

b:15.3
occ:1.00
O A:LEU175 2.7 10.1 1.0
O2A A:MYA1001 2.8 7.6 1.0
N A:LYS178 2.9 10.3 1.0
N A:LEU180 3.1 8.8 1.0
O4A A:MYA1001 3.1 8.3 1.0
N A:ARG179 3.3 9.1 1.0
CB A:LEU180 3.4 9.8 1.0
N A:GLU177 3.4 10.1 1.0
CA A:LYS178 3.5 11.2 1.0
C A:LYS178 3.5 11.5 1.0
CB A:LYS178 3.6 11.6 1.0
P1A A:MYA1001 3.7 8.2 1.0
O1A A:MYA1001 3.8 8.8 1.0
CA A:LEU180 3.8 9.0 1.0
C A:ARG176 3.8 10.4 1.0
C A:LEU175 3.9 9.2 1.0
CA A:ARG176 4.0 8.3 1.0
C A:GLU177 4.0 12.2 1.0
C A:ARG179 4.0 10.6 1.0
CG1 A:VAL171 4.0 8.7 1.0
CA A:ARG179 4.1 9.5 1.0
CA A:GLU177 4.2 12.2 1.0
P2A A:MYA1001 4.2 7.8 1.0
N A:ALA181 4.3 7.9 1.0
O A:LYS178 4.3 13.1 1.0
O3A A:MYA1001 4.3 8.0 1.0
N A:ARG176 4.4 8.8 1.0
C A:LEU180 4.5 8.9 1.0
CG A:LYS178 4.6 15.5 1.0
O A:ARG176 4.7 11.8 1.0
CG2 A:VAL171 4.7 7.6 1.0
O6A A:MYA1001 4.7 6.9 1.0
CG A:LEU180 4.7 11.1 1.0
CB A:VAL171 4.9 6.5 1.0
O A:HOH2389 5.0 26.6 1.0
CD2 A:LEU180 5.0 11.7 1.0

Reference:

J.A.Brannigan, S.M.Roberts, A.S.Bell, J.A.Hutton, M.R.Hodgkinson, E.W.Tate, R.J.Leatherbarrow, D.F.Smith, A.J.Wilkinson. Diverse Modes of Binding in Structures of Leishmania Major N-Myristoyltransferase with Selective Inhibitors Iucrj V. 1 250 2014.
ISSN: ISSN 2052-2525
PubMed: 25075346
DOI: 10.1107/S2052252514013001
Page generated: Mon Aug 11 07:15:33 2025

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