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Fluorine in PDB 1a2n: Structure of the C115A Mutant of Mura Complexed with the Fluorinated Analog of the Reaction Tetrahedral Intermediate

Enzymatic activity of Structure of the C115A Mutant of Mura Complexed with the Fluorinated Analog of the Reaction Tetrahedral Intermediate

All present enzymatic activity of Structure of the C115A Mutant of Mura Complexed with the Fluorinated Analog of the Reaction Tetrahedral Intermediate:
2.5.1.7;

Protein crystallography data

The structure of Structure of the C115A Mutant of Mura Complexed with the Fluorinated Analog of the Reaction Tetrahedral Intermediate, PDB code: 1a2n was solved by T.Skarzynski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.80
Space group P 3 2 1
Cell size a, b, c (Å), α, β, γ (°) 111.150, 111.150, 67.510, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Structure of the C115A Mutant of Mura Complexed with the Fluorinated Analog of the Reaction Tetrahedral Intermediate (pdb code 1a2n). 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 Structure of the C115A Mutant of Mura Complexed with the Fluorinated Analog of the Reaction Tetrahedral Intermediate, PDB code: 1a2n:

Fluorine binding site 1 out of 1 in 1a2n

Go back to Fluorine Binding Sites List in 1a2n
Fluorine binding site 1 out of 1 in the Structure of the C115A Mutant of Mura Complexed with the Fluorinated Analog of the Reaction Tetrahedral Intermediate


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Structure of the C115A Mutant of Mura Complexed with the Fluorinated Analog of the Reaction Tetrahedral Intermediate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F420

b:10.7
occ:1.00
F1 A:TET420 0.0 10.7 1.0
C19 A:TET420 1.3 21.2 1.0
C11 A:TET420 2.3 28.9 1.0
O21 A:TET420 2.6 29.1 1.0
C13 A:TET420 2.7 24.8 1.0
O22 A:TET420 2.8 25.1 1.0
C14 A:TET420 3.0 30.6 1.0
C20 A:TET420 3.0 25.1 1.0
O19 A:TET420 3.1 33.1 1.0
OD1 A:ASP305 3.2 13.3 1.0
O13 A:TET420 3.4 35.9 1.0
NH2 A:ARG331 3.7 7.4 1.0
O17 A:TET420 3.7 39.2 1.0
CD1 A:ILE117 3.7 17.1 1.0
CZ A:PHE328 3.8 23.1 1.0
CE2 A:PHE328 3.9 22.8 1.0
P3 A:TET420 3.9 39.0 1.0
C16 A:TET420 4.0 23.9 1.0
NH1 A:ARG331 4.1 6.9 1.0
C18 A:TET420 4.1 20.1 1.0
CZ A:ARG331 4.2 8.5 1.0
NH2 A:ARG120 4.2 13.0 1.0
CG A:ASP305 4.2 14.2 1.0
O18 A:TET420 4.3 31.6 1.0
O16 A:TET420 4.3 41.8 1.0
NH1 A:ARG120 4.4 12.1 1.0
CZ A:ARG120 4.5 14.7 1.0
N3 A:TET420 4.5 17.4 1.0
OD2 A:ASP305 4.5 9.6 1.0
O8 A:TET420 4.8 20.5 1.0
O A:HOH541 4.9 11.5 1.0
CE1 A:PHE328 4.9 22.9 1.0
CD2 A:PHE328 4.9 20.7 1.0
C10 A:TET420 4.9 20.4 1.0
C17 A:TET420 5.0 24.0 1.0

Reference:

T.Skarzynski, D.H.Kim, W.J.Lees, C.T.Walsh, K.Duncan. Stereochemical Course of Enzymatic Enolpyruvyl Transfer and Catalytic Conformation of the Active Site Revealed By the Crystal Structure of the Fluorinated Analogue of the Reaction Tetrahedral Intermediate Bound to the Active Site of the C115A Mutant of Mura Biochemistry V. 37 2572 1998.
ISSN: ISSN 0006-2960
PubMed: 9485407
DOI: 10.1021/BI9722608
Page generated: Sun Dec 13 11:28:03 2020

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