Atomistry » Fluorine » PDB 5msb-5njh » 5mu6
Atomistry »
  Fluorine »
    PDB 5msb-5njh »
      5mu6 »

Fluorine in PDB 5mu6: Human N-Myristoyltransferase (NMT1) with Myristoyl-Coa and Imp-1088 Inhibitor Bound

Enzymatic activity of Human N-Myristoyltransferase (NMT1) with Myristoyl-Coa and Imp-1088 Inhibitor Bound

All present enzymatic activity of Human N-Myristoyltransferase (NMT1) with Myristoyl-Coa and Imp-1088 Inhibitor Bound:
2.3.1.97;

Protein crystallography data

The structure of Human N-Myristoyltransferase (NMT1) with Myristoyl-Coa and Imp-1088 Inhibitor Bound, PDB code: 5mu6 was solved by I.Perez-Dorado, A.S.Bell, E.W.Tate, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 72.18 / 1.88
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 78.730, 180.730, 58.990, 90.00, 90.00, 90.00
R / Rfree (%) 20.4 / 24.7

Other elements in 5mu6:

The structure of Human N-Myristoyltransferase (NMT1) with Myristoyl-Coa and Imp-1088 Inhibitor Bound also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Human N-Myristoyltransferase (NMT1) with Myristoyl-Coa and Imp-1088 Inhibitor Bound (pdb code 5mu6). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the Human N-Myristoyltransferase (NMT1) with Myristoyl-Coa and Imp-1088 Inhibitor Bound, PDB code: 5mu6:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in 5mu6

Go back to Fluorine Binding Sites List in 5mu6
Fluorine binding site 1 out of 4 in the Human N-Myristoyltransferase (NMT1) with Myristoyl-Coa and Imp-1088 Inhibitor Bound


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Human N-Myristoyltransferase (NMT1) with Myristoyl-Coa and Imp-1088 Inhibitor Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F505

b:11.8
occ:1.00
 FAY A:KFK505 0.0 11.8 1.0
CAN A:KFK505 1.3 8.8 1.0
CAM A:KFK505 2.4 9.9 1.0
CAO A:KFK505 2.4 9.3 1.0
FAX A:KFK505 2.7 9.5 1.0
N A:ALA452 3.1 7.0 1.0
CB A:ASN451 3.1 8.5 1.0
C A:ASN451 3.2 7.5 1.0
CA A:ALA452 3.4 6.3 1.0
C A:ALA452 3.4 8.2 1.0
O A:HOH617 3.6 19.7 1.0
CAI A:KFK505 3.6 13.1 1.0
O A:ASN451 3.6 10.9 1.0
CAP A:KFK505 3.6 10.1 1.0
CA A:ASN451 3.7 6.9 1.0
O A:ALA452 3.8 9.8 1.0
N A:LEU453 3.8 11.8 1.0
CD2 A:TYR420 3.9 5.4 1.0
CB A:TYR296 4.2 11.6 1.0
CAQ A:KFK505 4.2 7.6 1.0
CE2 A:TYR420 4.2 7.7 1.0
O A:HOH780 4.3 18.5 1.0
CG A:ASN451 4.3 10.9 1.0
CG A:LEU453 4.4 10.3 1.0
O A:TRP297 4.5 11.5 1.0
CA A:LEU453 4.6 7.6 1.0
OAH A:KFK505 4.7 10.8 1.0
CD2 A:LEU453 4.8 12.8 1.0
CB A:ALA452 4.9 10.1 1.0
ND2 A:ASN451 4.9 9.3 1.0
CA A:TYR296 4.9 9.4 1.0
CG A:TYR420 4.9 7.0 1.0

Fluorine binding site 2 out of 4 in 5mu6

Go back to Fluorine Binding Sites List in 5mu6
Fluorine binding site 2 out of 4 in the Human N-Myristoyltransferase (NMT1) with Myristoyl-Coa and Imp-1088 Inhibitor Bound


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Human N-Myristoyltransferase (NMT1) with Myristoyl-Coa and Imp-1088 Inhibitor Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F505

b:9.5
occ:1.00
 FAX A:KFK505 0.0 9.5 1.0
CAM A:KFK505 1.4 9.9 1.0
CAN A:KFK505 2.4 8.8 1.0
CAI A:KFK505 2.4 13.1 1.0
OAH A:KFK505 2.7 10.8 1.0
FAY A:KFK505 2.7 11.8 1.0
CB A:ASN451 3.2 8.5 1.0
CE1 A:HIS298 3.3 10.6 1.0
CB A:TYR296 3.4 11.6 1.0
CAG A:KFK505 3.4 9.9 1.0
CG A:ASN451 3.5 10.9 1.0
ND1 A:HIS298 3.6 7.7 1.0
CAO A:KFK505 3.7 9.3 1.0
CAQ A:KFK505 3.7 7.6 1.0
OD1 A:ASN451 3.8 9.5 1.0
CG A:TYR296 3.9 8.8 1.0
ND2 A:ASN451 4.0 9.3 1.0
CD1 A:TYR296 4.0 12.6 1.0
CAP A:KFK505 4.1 10.1 1.0
O A:TRP297 4.2 11.5 1.0
CE2 A:TYR420 4.2 7.7 1.0
CAF A:KFK505 4.3 7.6 1.0
CA A:ASN451 4.3 6.9 1.0
NE2 A:HIS298 4.5 9.2 1.0
CA A:TYR296 4.6 9.4 1.0
N A:ALA452 4.6 7.0 1.0
N A:TRP297 4.7 9.0 1.0
C A:ASN451 4.7 7.5 1.0
CD2 A:TYR420 4.8 5.4 1.0
CD2 A:TYR296 4.8 10.4 1.0
C A:TYR296 4.8 9.1 1.0
CG A:HIS298 4.9 6.4 1.0
C A:TRP297 4.9 10.2 1.0
CZ A:TYR420 5.0 9.9 1.0

Fluorine binding site 3 out of 4 in 5mu6

Go back to Fluorine Binding Sites List in 5mu6
Fluorine binding site 3 out of 4 in the Human N-Myristoyltransferase (NMT1) with Myristoyl-Coa and Imp-1088 Inhibitor Bound


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Human N-Myristoyltransferase (NMT1) with Myristoyl-Coa and Imp-1088 Inhibitor Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F505

b:10.6
occ:1.00
 FAY B:KFK505 0.0 10.6 1.0
CAN B:KFK505 1.3 9.6 1.0
CAO B:KFK505 2.4 10.7 1.0
CAM B:KFK505 2.4 7.2 1.0
FAX B:KFK505 2.7 10.2 1.0
N B:ALA452 3.1 6.2 1.0
CB B:ASN451 3.2 7.5 1.0
C B:ASN451 3.2 8.3 1.0
CA B:ALA452 3.4 6.2 1.0
C B:ALA452 3.4 8.7 1.0
O B:ASN451 3.6 9.0 1.0
CAP B:KFK505 3.6 9.1 1.0
CAI B:KFK505 3.7 7.5 1.0
N B:LEU453 3.7 7.8 1.0
O B:ALA452 3.8 10.7 1.0
CA B:ASN451 3.8 8.7 1.0
CD2 B:TYR420 3.9 6.5 1.0
O B:HOH768 4.0 21.4 1.0
CB B:TYR296 4.2 9.2 1.0
CAQ B:KFK505 4.2 9.7 1.0
CE2 B:TYR420 4.2 7.4 1.0
CG B:LEU453 4.3 8.0 1.0
CG B:ASN451 4.4 9.6 1.0
O B:TRP297 4.5 11.0 1.0
CA B:LEU453 4.6 8.9 1.0
OAH B:KFK505 4.8 7.8 1.0
CD2 B:LEU453 4.8 10.4 1.0
O B:HOH718 4.9 11.7 1.0
CB B:ALA452 4.9 8.7 1.0
CA B:TYR296 4.9 9.6 1.0
CB B:LEU453 5.0 10.7 1.0
CG B:TYR420 5.0 10.2 1.0

Fluorine binding site 4 out of 4 in 5mu6

Go back to Fluorine Binding Sites List in 5mu6
Fluorine binding site 4 out of 4 in the Human N-Myristoyltransferase (NMT1) with Myristoyl-Coa and Imp-1088 Inhibitor Bound


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Human N-Myristoyltransferase (NMT1) with Myristoyl-Coa and Imp-1088 Inhibitor Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F505

b:10.2
occ:1.00
 FAX B:KFK505 0.0 10.2 1.0
CAM B:KFK505 1.3 7.2 1.0
CAN B:KFK505 2.4 9.6 1.0
CAI B:KFK505 2.4 7.5 1.0
FAY B:KFK505 2.7 10.6 1.0
OAH B:KFK505 2.7 7.8 1.0
CB B:ASN451 3.2 7.5 1.0
CE1 B:HIS298 3.4 10.9 1.0
CB B:TYR296 3.4 9.2 1.0
CG B:ASN451 3.5 9.6 1.0
CAG B:KFK505 3.5 10.3 1.0
CAO B:KFK505 3.6 10.7 1.0
CAQ B:KFK505 3.7 9.7 1.0
ND1 B:HIS298 3.7 9.6 1.0
OD1 B:ASN451 3.9 9.1 1.0
CG B:TYR296 3.9 10.6 1.0
ND2 B:ASN451 3.9 10.8 1.0
CAP B:KFK505 4.1 9.1 1.0
O B:TRP297 4.1 11.0 1.0
CD2 B:TYR296 4.1 11.6 1.0
CE2 B:TYR420 4.2 7.4 1.0
CA B:ASN451 4.3 8.7 1.0
CAF B:KFK505 4.4 10.6 1.0
NE2 B:HIS298 4.5 11.8 1.0
N B:ALA452 4.6 6.2 1.0
CA B:TYR296 4.6 9.6 1.0
N B:TRP297 4.6 8.3 1.0
C B:ASN451 4.7 8.3 1.0
CD2 B:TYR420 4.8 6.5 1.0
C B:TYR296 4.8 10.8 1.0
CD1 B:TYR296 4.9 11.8 1.0
C B:TRP297 4.9 7.1 1.0
CZ B:TYR420 4.9 6.4 1.0
CG B:HIS298 4.9 10.3 1.0
OH B:TYR420 5.0 10.5 1.0

Reference:

A.Mousnier, A.S.Bell, D.P.Swieboda, J.Morales-Sanfrutos, I.Perez-Dorado, J.A.Brannigan, J.Newman, M.Ritzefeld, J.A.Hutton, A.Guedan, A.S.Asfor, S.W.Robinson, I.Hopkins-Navratilova, A.J.Wilkinson, S.L.Johnston, R.J.Leatherbarrow, T.J.Tuthill, R.Solari, E.W.Tate. Fragment-Derived Inhibitors of Human N-Myristoyltransferase Block Capsid Assembly and Replication of the Common Cold Virus. Nat Chem V. 10 599 2018.
ISSN: ESSN 1755-4349
PubMed: 29760414
DOI: 10.1038/S41557-018-0039-2
Page generated: Thu Aug 1 11:51:36 2024

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy