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Magnesium in PDB 6ehj: Human N-Myristoyltransferase (NMT1) with Myristoyl-Coa and Peptide Bound

Enzymatic activity of Human N-Myristoyltransferase (NMT1) with Myristoyl-Coa and Peptide Bound

All present enzymatic activity of Human N-Myristoyltransferase (NMT1) with Myristoyl-Coa and Peptide Bound:
2.3.1.97; 2.7.10.2;

Protein crystallography data

The structure of Human N-Myristoyltransferase (NMT1) with Myristoyl-Coa and Peptide Bound, PDB code: 6ehj was solved by I.Perez-Dorado, M.Ritzefeld, E.W.Tate, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.08 / 2.10
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 80.250, 177.540, 58.140, 90.00, 90.00, 90.00
R / Rfree (%) 19.3 / 23.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Human N-Myristoyltransferase (NMT1) with Myristoyl-Coa and Peptide Bound (pdb code 6ehj). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Human N-Myristoyltransferase (NMT1) with Myristoyl-Coa and Peptide Bound, PDB code: 6ehj:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 6ehj

Go back to Magnesium Binding Sites List in 6ehj
Magnesium binding site 1 out of 2 in the Human N-Myristoyltransferase (NMT1) with Myristoyl-Coa and Peptide Bound


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human N-Myristoyltransferase (NMT1) with Myristoyl-Coa and Peptide Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg501

b:51.9
occ:1.00
O A:LEU254 2.6 48.8 1.0
N A:LYS257 2.8 51.9 1.0
N A:VAL259 3.0 36.7 1.0
O2A D:MYA2601 3.0 48.7 1.0
O4A D:MYA2601 3.1 52.9 1.0
N A:ARG258 3.2 45.1 1.0
C A:LYS257 3.3 47.9 1.0
CA A:LYS257 3.3 52.1 1.0
CG2 A:VAL259 3.4 39.1 1.0
CB A:VAL259 3.4 38.3 1.0
N A:SER256 3.5 53.1 1.0
CB A:LYS257 3.6 52.8 1.0
C A:LEU254 3.7 41.9 1.0
C A:ARG255 3.7 53.9 1.0
CA A:VAL259 3.8 36.7 1.0
CA A:ARG255 3.9 50.8 1.0
C A:SER256 3.9 57.3 1.0
O A:LYS257 4.0 48.7 1.0
C A:ARG258 4.0 38.2 1.0
O1A D:MYA2601 4.1 52.1 1.0
P1A D:MYA2601 4.1 60.4 1.0
CA A:ARG258 4.1 47.4 1.0
CG1 A:VAL250 4.1 33.0 1.0
CA A:SER256 4.1 56.7 1.0
N A:ARG255 4.2 47.0 1.0
N A:ALA260 4.3 28.8 1.0
O A:ARG255 4.3 59.4 1.0
P2A D:MYA2601 4.3 58.3 1.0
C A:VAL259 4.6 31.9 1.0
O3A D:MYA2601 4.7 54.6 1.0
CB A:LEU254 4.8 41.7 1.0
CG1 A:VAL259 4.8 34.8 1.0
CA A:LEU254 4.8 41.8 1.0
O6A D:MYA2601 4.9 55.0 1.0
CG A:LYS257 4.9 57.4 1.0
CG2 A:VAL250 5.0 27.1 1.0

Magnesium binding site 2 out of 2 in 6ehj

Go back to Magnesium Binding Sites List in 6ehj
Magnesium binding site 2 out of 2 in the Human N-Myristoyltransferase (NMT1) with Myristoyl-Coa and Peptide Bound


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Human N-Myristoyltransferase (NMT1) with Myristoyl-Coa and Peptide Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg501

b:49.8
occ:1.00
O4A B:COA502 2.5 53.0 1.0
N B:LYS257 2.7 56.6 1.0
O B:LEU254 2.8 52.3 1.0
N B:VAL259 2.8 46.1 1.0
O2A B:COA502 3.0 54.2 1.0
N B:ARG258 3.2 51.6 1.0
CG2 B:VAL259 3.3 47.9 1.0
CB B:VAL259 3.3 44.5 1.0
C B:LYS257 3.4 51.9 1.0
CA B:LYS257 3.4 56.4 1.0
N B:SER256 3.4 55.5 1.0
CA B:VAL259 3.6 43.4 1.0
CB B:LYS257 3.6 54.5 1.0
C B:ARG255 3.8 55.7 1.0
C B:SER256 3.8 56.9 1.0
C B:ARG258 3.8 48.7 1.0
C B:LEU254 3.9 50.3 1.0
CA B:SER256 4.0 57.0 1.0
P2A B:COA502 4.0 55.8 1.0
CA B:ARG258 4.0 54.1 1.0
CA B:ARG255 4.1 51.0 1.0
O B:LYS257 4.1 48.8 1.0
N B:ALA260 4.2 45.3 1.0
P1A B:COA502 4.2 59.9 1.0
CG B:LYS257 4.3 55.0 1.0
CG1 B:VAL250 4.3 42.4 1.0
C B:VAL259 4.4 43.5 1.0
O B:ARG255 4.5 54.3 1.0
N B:ARG255 4.5 48.9 1.0
O3A B:COA502 4.6 50.2 1.0
O5A B:COA502 4.6 54.6 1.0
O1A B:COA502 4.7 59.0 1.0
CG1 B:VAL259 4.8 41.9 1.0
O B:SER256 4.9 59.0 1.0
O6A B:COA502 5.0 50.0 1.0
O B:ARG258 5.0 50.8 1.0

Reference:

I.Perez-Dorado, M.Ritzefeld, E.W.Tate. Human N-Myristoyltransferase (NMT1) with Myristoyl-Coa and Peptide Bound To Be Published.
Page generated: Mon Sep 30 23:57:42 2024

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