Atomistry » Fluorine » PDB 4bkz-4c62 » 4c5s
Atomistry »
  Fluorine »
    PDB 4bkz-4c62 »
      4c5s »

Fluorine in PDB 4c5s: Structural Investigations Into the Stereochemistry and Activity of A Phenylalanine-2,3-Aminomutase From Taxus Chinensis

Enzymatic activity of Structural Investigations Into the Stereochemistry and Activity of A Phenylalanine-2,3-Aminomutase From Taxus Chinensis

All present enzymatic activity of Structural Investigations Into the Stereochemistry and Activity of A Phenylalanine-2,3-Aminomutase From Taxus Chinensis:
4.3.1.24;

Protein crystallography data

The structure of Structural Investigations Into the Stereochemistry and Activity of A Phenylalanine-2,3-Aminomutase From Taxus Chinensis, PDB code: 4c5s was solved by G.G.Wybenga, W.Szymanski, B.Wu, B.L.Feringa, D.B.Janssen, B.W.Dijkstra, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 99.07 / 1.85
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 99.751, 146.185, 100.395, 90.00, 99.31, 90.00
R / Rfree (%) 17.835 / 20.528

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Structural Investigations Into the Stereochemistry and Activity of A Phenylalanine-2,3-Aminomutase From Taxus Chinensis (pdb code 4c5s). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 8 binding sites of Fluorine where determined in the Structural Investigations Into the Stereochemistry and Activity of A Phenylalanine-2,3-Aminomutase From Taxus Chinensis, PDB code: 4c5s:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Fluorine binding site 1 out of 8 in 4c5s

Go back to Fluorine Binding Sites List in 4c5s
Fluorine binding site 1 out of 8 in the Structural Investigations Into the Stereochemistry and Activity of A Phenylalanine-2,3-Aminomutase From Taxus Chinensis


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Structural Investigations Into the Stereochemistry and Activity of A Phenylalanine-2,3-Aminomutase From Taxus Chinensis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F1678

b:24.6
occ:1.00
 FR A:BQ71678 0.0 24.6 1.0
CA A:BQ71678 1.3 22.9 1.0
FS A:BQ71678 2.1 24.6 1.0
CB A:BQ71678 2.3 23.2 1.0
C A:BQ71678 2.4 21.5 1.0
O1 A:BQ71678 2.7 20.1 1.0
O A:HOH2216 2.8 17.6 1.0
CG A:BQ71678 2.8 20.6 1.0
N A:GLY87 2.9 14.7 1.0
O A:HOH2030 2.9 16.7 1.0
CA A:GLY87 3.3 15.0 1.0
O A:BQ71678 3.4 20.8 1.0
CD1 A:BQ71678 3.4 19.9 1.0
N A:BQ71678 3.6 23.0 1.0
CD2 A:BQ71678 3.6 20.3 1.0
O A:HOH2031 3.7 22.0 1.0
O A:HOH2028 3.7 22.0 1.0
C A:PHE86 4.0 14.5 1.0
NE2 B:GLN319 4.1 15.4 1.0
CA A:PHE86 4.3 14.8 1.0
CE1 A:BQ71678 4.5 20.1 1.0
C A:GLY87 4.5 15.0 1.0
CE2 A:BQ71678 4.6 19.2 1.0
CB A:PHE86 4.7 14.8 1.0
CB2 A:MDO175 4.7 23.1 1.0
O A:GLY87 4.7 14.6 1.0
ND2 A:ASN458 4.9 14.4 1.0
CZ A:BQ71678 5.0 19.4 1.0

Fluorine binding site 2 out of 8 in 4c5s

Go back to Fluorine Binding Sites List in 4c5s
Fluorine binding site 2 out of 8 in the Structural Investigations Into the Stereochemistry and Activity of A Phenylalanine-2,3-Aminomutase From Taxus Chinensis


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Structural Investigations Into the Stereochemistry and Activity of A Phenylalanine-2,3-Aminomutase From Taxus Chinensis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F1678

b:24.6
occ:1.00
 FS A:BQ71678 0.0 24.6 1.0
CA A:BQ71678 1.3 22.9 1.0
FR A:BQ71678 2.1 24.6 1.0
C A:BQ71678 2.3 21.5 1.0
CB A:BQ71678 2.4 23.2 1.0
O A:BQ71678 2.6 20.8 1.0
CD2 A:BQ71678 2.8 20.3 1.0
CG A:BQ71678 2.8 20.6 1.0
O A:HOH2028 3.2 22.0 1.0
N A:BQ71678 3.2 23.0 1.0
CD1 A:LEU227 3.3 14.7 1.0
O1 A:BQ71678 3.4 20.1 1.0
ND2 A:ASN231 3.8 14.6 1.0
O A:HOH2030 3.8 16.7 1.0
CE2 A:BQ71678 4.0 19.2 1.0
CD1 A:BQ71678 4.0 19.9 1.0
OD1 A:ASN231 4.1 15.8 1.0
CD2 A:LEU227 4.1 14.9 1.0
CG A:ASN231 4.2 15.7 1.0
CG A:LEU227 4.3 15.0 1.0
CB2 A:MDO175 4.4 23.1 1.0
CD1 A:PHE86 4.4 15.4 1.0
N A:GLY87 4.4 14.7 1.0
O A:HOH2216 4.7 17.6 1.0
CB A:PHE86 4.8 14.8 1.0
CA A:PHE86 4.9 14.8 1.0
CZ A:BQ71678 4.9 19.4 1.0
CE1 A:BQ71678 5.0 20.1 1.0

Fluorine binding site 3 out of 8 in 4c5s

Go back to Fluorine Binding Sites List in 4c5s
Fluorine binding site 3 out of 8 in the Structural Investigations Into the Stereochemistry and Activity of A Phenylalanine-2,3-Aminomutase From Taxus Chinensis


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Structural Investigations Into the Stereochemistry and Activity of A Phenylalanine-2,3-Aminomutase From Taxus Chinensis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F1678

b:23.6
occ:1.00
 FR B:BQ71678 0.0 23.6 1.0
CA B:BQ71678 1.3 22.0 1.0
FS B:BQ71678 2.1 22.8 1.0
CB B:BQ71678 2.2 21.9 1.0
C B:BQ71678 2.3 21.7 1.0
O1 B:BQ71678 2.7 20.9 1.0
O A:HOH2130 2.8 17.9 1.0
CG B:BQ71678 2.8 20.6 1.0
N B:GLY87 2.9 16.6 1.0
O B:HOH2035 3.0 14.2 1.0
CA B:GLY87 3.3 16.2 1.0
O B:BQ71678 3.3 21.1 1.0
CD1 B:BQ71678 3.5 19.7 1.0
N B:BQ71678 3.6 22.0 1.0
CD2 B:BQ71678 3.6 19.7 1.0
O A:HOH2123 3.7 21.4 1.0
O A:HOH2124 3.8 20.2 1.0
C B:PHE86 4.1 16.1 1.0
NE2 A:GLN319 4.2 15.1 1.0
CA B:PHE86 4.4 16.8 1.0
CE1 B:BQ71678 4.6 19.1 1.0
C B:GLY87 4.6 15.9 1.0
CE2 B:BQ71678 4.6 19.2 1.0
CB B:PHE86 4.7 16.4 1.0
CB2 B:MDO175 4.7 23.0 1.0
O B:GLY87 4.8 15.4 1.0
ND2 B:ASN458 4.9 14.0 1.0

Fluorine binding site 4 out of 8 in 4c5s

Go back to Fluorine Binding Sites List in 4c5s
Fluorine binding site 4 out of 8 in the Structural Investigations Into the Stereochemistry and Activity of A Phenylalanine-2,3-Aminomutase From Taxus Chinensis


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Structural Investigations Into the Stereochemistry and Activity of A Phenylalanine-2,3-Aminomutase From Taxus Chinensis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F1678

b:22.8
occ:1.00
 FS B:BQ71678 0.0 22.8 1.0
CA B:BQ71678 1.3 22.0 1.0
FR B:BQ71678 2.1 23.6 1.0
C B:BQ71678 2.3 21.7 1.0
CB B:BQ71678 2.4 21.9 1.0
O B:BQ71678 2.6 21.1 1.0
CD2 B:BQ71678 2.8 19.7 1.0
CG B:BQ71678 2.8 20.6 1.0
N B:BQ71678 3.1 22.0 1.0
O A:HOH2123 3.3 21.4 1.0
O1 B:BQ71678 3.5 20.9 1.0
CD1 B:LEU227 3.5 12.7 1.0
ND2 B:ASN231 3.5 14.8 1.0
O B:HOH2035 4.0 14.2 1.0
CE2 B:BQ71678 4.0 19.2 1.0
OD1 B:ASN231 4.0 16.1 1.0
CD1 B:BQ71678 4.1 19.7 1.0
CG B:ASN231 4.1 15.2 1.0
CD2 B:LEU227 4.1 12.7 1.0
CG B:LEU227 4.3 13.3 1.0
CB2 B:MDO175 4.4 23.0 1.0
N B:GLY87 4.5 16.6 1.0
CD1 B:PHE86 4.6 16.5 1.0
O A:HOH2130 4.8 17.9 1.0
CB B:PHE86 4.9 16.4 1.0
CZ B:BQ71678 5.0 19.5 1.0
CE1 B:BQ71678 5.0 19.1 1.0

Fluorine binding site 5 out of 8 in 4c5s

Go back to Fluorine Binding Sites List in 4c5s
Fluorine binding site 5 out of 8 in the Structural Investigations Into the Stereochemistry and Activity of A Phenylalanine-2,3-Aminomutase From Taxus Chinensis


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 5 of Structural Investigations Into the Stereochemistry and Activity of A Phenylalanine-2,3-Aminomutase From Taxus Chinensis within 5.0Å range:
probe atom residue distance (Å) B Occ
C:F1678

b:25.3
occ:1.00
 FR C:BQ71678 0.0 25.3 1.0
CA C:BQ71678 1.3 22.9 1.0
FS C:BQ71678 2.1 25.2 1.0
CB C:BQ71678 2.3 22.4 1.0
C C:BQ71678 2.3 23.1 1.0
O1 C:BQ71678 2.7 22.3 1.0
O C:HOH2170 2.8 21.2 1.0
CG C:BQ71678 2.8 20.0 1.0
N C:GLY87 2.9 17.0 1.0
O C:HOH2030 3.0 15.8 1.0
CA C:GLY87 3.3 17.1 1.0
O C:BQ71678 3.3 22.3 1.0
CD1 C:BQ71678 3.5 19.4 1.0
N C:BQ71678 3.6 21.5 1.0
CD2 C:BQ71678 3.6 19.3 1.0
O C:HOH2028 3.7 20.3 1.0
O C:HOH2031 3.7 22.1 1.0
C C:PHE86 4.0 17.2 1.0
NE2 D:GLN319 4.0 14.2 1.0
CA C:PHE86 4.3 17.4 1.0
C C:GLY87 4.5 17.6 1.0
CE1 C:BQ71678 4.6 18.7 1.0
CE2 C:BQ71678 4.6 19.0 1.0
O C:GLY87 4.7 16.8 1.0
CB2 C:MDO175 4.7 21.5 1.0
CB C:PHE86 4.8 17.8 1.0
ND2 C:ASN458 4.9 14.6 1.0

Fluorine binding site 6 out of 8 in 4c5s

Go back to Fluorine Binding Sites List in 4c5s
Fluorine binding site 6 out of 8 in the Structural Investigations Into the Stereochemistry and Activity of A Phenylalanine-2,3-Aminomutase From Taxus Chinensis


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 6 of Structural Investigations Into the Stereochemistry and Activity of A Phenylalanine-2,3-Aminomutase From Taxus Chinensis within 5.0Å range:
probe atom residue distance (Å) B Occ
C:F1678

b:25.2
occ:1.00
 FS C:BQ71678 0.0 25.2 1.0
CA C:BQ71678 1.3 22.9 1.0
FR C:BQ71678 2.1 25.3 1.0
C C:BQ71678 2.3 23.1 1.0
CB C:BQ71678 2.4 22.4 1.0
O C:BQ71678 2.5 22.3 1.0
CD2 C:BQ71678 2.8 19.3 1.0
CG C:BQ71678 2.8 20.0 1.0
N C:BQ71678 3.2 21.5 1.0
O C:HOH2028 3.3 20.3 1.0
CD1 C:LEU227 3.4 14.4 1.0
O1 C:BQ71678 3.4 22.3 1.0
ND2 C:ASN231 3.7 15.6 1.0
O C:HOH2030 3.8 15.8 1.0
CE2 C:BQ71678 4.0 19.0 1.0
CD1 C:BQ71678 4.1 19.4 1.0
OD1 C:ASN231 4.1 17.0 1.0
CD2 C:LEU227 4.2 14.1 1.0
CG C:ASN231 4.2 16.1 1.0
CG C:LEU227 4.3 14.5 1.0
N C:GLY87 4.4 17.0 1.0
CB2 C:MDO175 4.4 21.5 1.0
CD1 C:PHE86 4.5 17.9 1.0
O C:HOH2170 4.7 21.2 1.0
CB C:PHE86 4.8 17.8 1.0
CA C:PHE86 4.9 17.4 1.0
CZ C:BQ71678 5.0 18.6 1.0
CE1 C:BQ71678 5.0 18.7 1.0

Fluorine binding site 7 out of 8 in 4c5s

Go back to Fluorine Binding Sites List in 4c5s
Fluorine binding site 7 out of 8 in the Structural Investigations Into the Stereochemistry and Activity of A Phenylalanine-2,3-Aminomutase From Taxus Chinensis


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 7 of Structural Investigations Into the Stereochemistry and Activity of A Phenylalanine-2,3-Aminomutase From Taxus Chinensis within 5.0Å range:
probe atom residue distance (Å) B Occ
D:F1678

b:21.2
occ:1.00
 FR D:BQ71678 0.0 21.2 1.0
CA D:BQ71678 1.3 20.2 1.0
FS D:BQ71678 2.2 22.1 1.0
CB D:BQ71678 2.2 19.9 1.0
C D:BQ71678 2.3 18.7 1.0
O1 D:BQ71678 2.7 17.8 1.0
CG D:BQ71678 2.8 18.2 1.0
O C:HOH2118 2.9 16.4 1.0
N D:GLY87 2.9 14.7 1.0
O C:HOH2113 3.0 17.6 1.0
O D:BQ71678 3.3 18.1 1.0
CA D:GLY87 3.3 14.6 1.0
CD1 D:BQ71678 3.4 18.3 1.0
CD2 D:BQ71678 3.5 18.1 1.0
N D:BQ71678 3.5 20.7 1.0
O C:HOH2112 3.7 17.6 1.0
O C:HOH2114 3.8 17.7 1.0
C D:PHE86 4.0 14.6 1.0
NE2 C:GLN319 4.2 15.4 1.0
CA D:PHE86 4.3 14.3 1.0
CE1 D:BQ71678 4.5 18.5 1.0
CE2 D:BQ71678 4.6 17.3 1.0
C D:GLY87 4.6 14.2 1.0
CB D:PHE86 4.7 13.7 1.0
CB2 D:MDO175 4.7 21.7 1.0
O D:GLY87 4.9 13.4 1.0
CZ D:BQ71678 5.0 17.8 1.0

Fluorine binding site 8 out of 8 in 4c5s

Go back to Fluorine Binding Sites List in 4c5s
Fluorine binding site 8 out of 8 in the Structural Investigations Into the Stereochemistry and Activity of A Phenylalanine-2,3-Aminomutase From Taxus Chinensis


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 8 of Structural Investigations Into the Stereochemistry and Activity of A Phenylalanine-2,3-Aminomutase From Taxus Chinensis within 5.0Å range:
probe atom residue distance (Å) B Occ
D:F1678

b:22.1
occ:1.00
 FS D:BQ71678 0.0 22.1 1.0
CA D:BQ71678 1.3 20.2 1.0
FR D:BQ71678 2.2 21.2 1.0
C D:BQ71678 2.4 18.7 1.0
CB D:BQ71678 2.4 19.9 1.0
O D:BQ71678 2.6 18.1 1.0
CD2 D:BQ71678 2.7 18.1 1.0
CG D:BQ71678 2.8 18.2 1.0
N D:BQ71678 3.1 20.7 1.0
CD1 D:LEU227 3.4 13.3 1.0
O C:HOH2112 3.4 17.6 1.0
O1 D:BQ71678 3.5 17.8 1.0
ND2 D:ASN231 3.6 14.3 1.0
OD1 D:ASN231 3.9 15.3 1.0
CE2 D:BQ71678 3.9 17.3 1.0
CG D:ASN231 4.0 13.9 1.0
CD1 D:BQ71678 4.1 18.3 1.0
O C:HOH2113 4.1 17.6 1.0
CD2 D:LEU227 4.1 13.7 1.0
CG D:LEU227 4.3 13.4 1.0
CB2 D:MDO175 4.3 21.7 1.0
N D:GLY87 4.5 14.7 1.0
CD1 D:PHE86 4.5 14.4 1.0
O C:HOH2118 4.8 16.4 1.0
CB D:PHE86 4.9 13.7 1.0
CZ D:BQ71678 4.9 17.8 1.0
CE1 D:BQ71678 5.0 18.5 1.0

Reference:

G.G.Wybenga, W.Szymanski, B.Wu, B.L.Feringa, D.B.Janssen, B.W.Dijkstra. Structural Investigations Into the Stereochemistry and Activity of A Phenylalanine-2,3-Aminomutase From Taxus Chinensis. Biochemistry V. 53 3187 2014.
ISSN: ISSN 0006-2960
PubMed: 24786474
DOI: 10.1021/BI500187A
Page generated: Sun Dec 13 12:00:04 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy