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Fluorine in PDB 4cn4: Glge Isoform 1 From Streptomyces Coelicolor E423A Mutant with 2-Deoxy-2-Fluoro-Beta-Maltosyl Modification

Enzymatic activity of Glge Isoform 1 From Streptomyces Coelicolor E423A Mutant with 2-Deoxy-2-Fluoro-Beta-Maltosyl Modification

All present enzymatic activity of Glge Isoform 1 From Streptomyces Coelicolor E423A Mutant with 2-Deoxy-2-Fluoro-Beta-Maltosyl Modification:
2.4.99.16;

Protein crystallography data

The structure of Glge Isoform 1 From Streptomyces Coelicolor E423A Mutant with 2-Deoxy-2-Fluoro-Beta-Maltosyl Modification, PDB code: 4cn4 was solved by K.Syson, C.E.M.Stevenson, A.M.Rashid, G.Saalbach, M.Tang, A.Tuukanen, D.I.Svergun, S.G.Withers, D.M.Lawson, S.Bornemann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.54 / 2.40
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 113.000, 113.000, 312.860, 90.00, 90.00, 90.00
R / Rfree (%) 18.4 / 20.848

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Glge Isoform 1 From Streptomyces Coelicolor E423A Mutant with 2-Deoxy-2-Fluoro-Beta-Maltosyl Modification (pdb code 4cn4). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Glge Isoform 1 From Streptomyces Coelicolor E423A Mutant with 2-Deoxy-2-Fluoro-Beta-Maltosyl Modification, PDB code: 4cn4:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in 4cn4

Go back to Fluorine Binding Sites List in 4cn4
Fluorine binding site 1 out of 2 in the Glge Isoform 1 From Streptomyces Coelicolor E423A Mutant with 2-Deoxy-2-Fluoro-Beta-Maltosyl Modification


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Glge Isoform 1 From Streptomyces Coelicolor E423A Mutant with 2-Deoxy-2-Fluoro-Beta-Maltosyl Modification within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F1394

b:47.8
occ:1.00
F2 A:SHG1394 0.0 47.8 1.0
C2 A:SHG1394 1.4 45.0 1.0
C1 A:SHG1394 2.4 46.5 1.0
C3 A:SHG1394 2.4 45.9 1.0
OD1 A:ASP394 3.0 43.1 1.0
O3 A:SHG1394 3.0 42.0 1.0
NH2 A:ARG392 3.1 35.9 1.0
OD2 A:ASP480 3.2 51.9 1.0
NH1 A:ARG392 3.6 39.4 1.0
O5 A:SHG1394 3.7 46.6 1.0
C4 A:SHG1394 3.8 45.2 1.0
CZ A:ARG392 3.8 35.8 1.0
O A:HOH2201 4.0 38.5 1.0
C5 A:SHG1394 4.0 46.2 1.0
CG A:ASP480 4.2 44.7 1.0
CG A:ASP394 4.2 38.4 1.0
CZ2 A:TRP281 4.4 31.1 1.0
O A:HOH2084 4.4 31.5 1.0
CE2 A:TRP281 4.4 31.4 1.0
NE1 A:TRP281 4.5 32.4 1.0
OD1 A:ASP480 4.6 45.9 1.0
OD2 A:ASP394 4.8 39.9 1.0
O4 A:SHG1394 4.9 44.0 1.0
CH2 A:TRP281 5.0 31.7 1.0

Fluorine binding site 2 out of 2 in 4cn4

Go back to Fluorine Binding Sites List in 4cn4
Fluorine binding site 2 out of 2 in the Glge Isoform 1 From Streptomyces Coelicolor E423A Mutant with 2-Deoxy-2-Fluoro-Beta-Maltosyl Modification


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Glge Isoform 1 From Streptomyces Coelicolor E423A Mutant with 2-Deoxy-2-Fluoro-Beta-Maltosyl Modification within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F1394

b:52.1
occ:1.00
F2 B:SHG1394 0.0 52.1 1.0
C2 B:SHG1394 1.4 51.6 1.0
C1 B:SHG1394 2.4 52.5 1.0
C3 B:SHG1394 2.4 52.5 1.0
O3 B:SHG1394 3.0 50.9 1.0
OD1 B:ASP394 3.0 48.9 1.0
NH2 B:ARG392 3.1 37.0 1.0
OD2 B:ASP480 3.2 53.2 1.0
NH1 B:ARG392 3.6 37.4 1.0
O5 B:SHG1394 3.7 54.5 1.0
C4 B:SHG1394 3.8 53.2 1.0
CZ B:ARG392 3.8 37.2 1.0
C5 B:SHG1394 4.1 54.6 1.0
O B:HOH2086 4.1 36.3 1.0
CG B:ASP480 4.2 50.6 1.0
CG B:ASP394 4.2 42.8 1.0
CZ2 B:TRP281 4.4 35.7 1.0
CE2 B:TRP281 4.4 36.1 1.0
NE1 B:TRP281 4.5 36.0 1.0
O B:HOH2156 4.5 46.0 1.0
OD1 B:ASP480 4.6 51.4 1.0
O B:HOH2123 4.7 52.2 1.0
OD2 B:ASP394 4.7 42.5 1.0
O4 B:SHG1394 4.9 51.9 1.0
CH2 B:TRP281 5.0 35.9 1.0

Reference:

K.Syson, C.E.M.Stevenson, A.M.Rashid, G.Saalbach, M.Tang, A.Tuukkanen, D.I.Svergun, S.G.Withers, D.M.Lawson, S.Bornemann. Structural Insight Into How Streptomyces Coelicolor Maltosyl Transferase Glge Binds Alpha-Maltose 1-Phosphate and Forms A Maltosyl-Enzyme Intermediate. Biochemistry V. 53 2494 2014.
ISSN: ISSN 0006-2960
PubMed: 24689960
DOI: 10.1021/BI500183C
Page generated: Thu Aug 1 00:45:49 2024

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