Fluorine in PDB 5swn: Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - ASP110ASN/Fluoroacetate - Cocrystallized

Enzymatic activity of Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - ASP110ASN/Fluoroacetate - Cocrystallized

All present enzymatic activity of Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - ASP110ASN/Fluoroacetate - Cocrystallized:
3.8.1.3;

Protein crystallography data

The structure of Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - ASP110ASN/Fluoroacetate - Cocrystallized, PDB code: 5swn was solved by P.Mehrabi, T.H.Kim, S.R.Prosser, E.F.Pai, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.78 / 1.54
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 41.880, 78.870, 84.900, 90.00, 103.18, 90.00
R / Rfree (%) 16.9 / 19.4

Other elements in 5swn:

The structure of Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - ASP110ASN/Fluoroacetate - Cocrystallized also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - ASP110ASN/Fluoroacetate - Cocrystallized (pdb code 5swn). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - ASP110ASN/Fluoroacetate - Cocrystallized, PDB code: 5swn:

Fluorine binding site 1 out of 1 in 5swn

Go back to Fluorine Binding Sites List in 5swn
Fluorine binding site 1 out of 1 in the Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - ASP110ASN/Fluoroacetate - Cocrystallized


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - ASP110ASN/Fluoroacetate - Cocrystallized within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F401

b:25.7
occ:1.00
 F A:FAH401 0.0 25.7 1.0
CH3 A:FAH401 1.5 16.6 1.0
C A:FAH401 2.4 15.6 1.0
OXT A:FAH401 2.5 28.6 1.0
NE2 A:HIS155 3.0 21.0 1.0
NE1 A:TRP156 3.2 12.4 1.0
CE1 A:HIS155 3.3 20.7 1.0
OH A:TYR219 3.5 12.1 1.0
O A:FAH401 3.5 12.9 1.0
CD1 A:ILE253 3.7 16.9 1.0
ND2 A:ASN110 3.9 11.1 1.0
CD1 A:TRP156 4.1 11.8 1.0
CH2 A:TRP185 4.2 21.2 1.0
CE2 A:TRP156 4.2 9.2 1.0
CD2 A:HIS155 4.2 18.8 1.0
CZ2 A:TRP156 4.5 10.4 1.0
CZ A:TYR219 4.5 10.6 1.0
O A:HOH616 4.5 19.0 1.0
CZ3 A:TRP185 4.6 19.9 1.0
CE1 A:TYR219 4.6 10.9 1.0
CG A:ASN110 4.6 7.5 1.0
CZ2 A:TRP185 4.6 18.5 1.0
ND1 A:HIS155 4.7 21.8 1.0
OD1 A:ASN110 4.8 7.5 1.0
CG2 A:ILE253 4.9 22.7 1.0

Reference:

T.H.Kim, P.Mehrabi, Z.Ren, A.Sljoka, C.Ing, A.Bezginov, L.Ye, R.Pomes, R.S.Prosser, E.F.Pai. The Role of Dimer Asymmetry and Protomer Dynamics in Enzyme Catalysis. Science V. 355 2017.
ISSN: ESSN 1095-9203
PubMed: 28104837
DOI: 10.1126/SCIENCE.AAG2355
Page generated: Sun Dec 13 12:37:33 2020

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