Atomistry » Fluorine » PDB 1h2j-1j97 » 1if5
Atomistry »
  Fluorine »
    PDB 1h2j-1j97 »
      1if5 »

Fluorine in PDB 1if5: Carbonic Anhydrase II Complexed with 2,6-Difluorobenzenesulfonamide

Enzymatic activity of Carbonic Anhydrase II Complexed with 2,6-Difluorobenzenesulfonamide

All present enzymatic activity of Carbonic Anhydrase II Complexed with 2,6-Difluorobenzenesulfonamide:
4.2.1.1;

Protein crystallography data

The structure of Carbonic Anhydrase II Complexed with 2,6-Difluorobenzenesulfonamide, PDB code: 1if5 was solved by C.-Y.Kim, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 43.200, 42.700, 73.300, 90.00, 104.58, 90.00
R / Rfree (%) 22.1 / 28.7

Other elements in 1if5:

The structure of Carbonic Anhydrase II Complexed with 2,6-Difluorobenzenesulfonamide also contains other interesting chemical elements:

Mercury (Hg) 1 atom
Zinc (Zn) 1 atom

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Carbonic Anhydrase II Complexed with 2,6-Difluorobenzenesulfonamide (pdb code 1if5). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Carbonic Anhydrase II Complexed with 2,6-Difluorobenzenesulfonamide, PDB code: 1if5:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in 1if5

Go back to Fluorine Binding Sites List in 1if5
Fluorine binding site 1 out of 2 in the Carbonic Anhydrase II Complexed with 2,6-Difluorobenzenesulfonamide


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Carbonic Anhydrase II Complexed with 2,6-Difluorobenzenesulfonamide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F555

b:17.9
occ:1.00
F11 A:FBT555 0.0 17.9 1.0
C03 A:FBT555 1.4 14.0 1.0
C02 A:FBT555 2.4 14.9 1.0
C04 A:FBT555 2.4 13.3 1.0
OG1 A:THR200 2.9 14.3 1.0
NP0 A:FBT555 3.0 12.9 1.0
S07 A:FBT555 3.0 10.3 1.0
CG2 A:THR200 3.2 11.6 1.0
O08 A:FBT555 3.3 10.5 1.0
N A:THR200 3.4 10.2 1.0
CB A:THR200 3.5 10.6 1.0
C01 A:FBT555 3.7 14.7 1.0
C05 A:FBT555 3.7 11.5 1.0
N A:THR199 3.8 11.4 1.0
CA A:THR200 3.9 10.6 1.0
OG1 A:THR199 4.1 13.6 1.0
CB A:LEU198 4.2 9.9 1.0
C A:THR199 4.2 9.6 1.0
C06 A:FBT555 4.2 16.1 1.0
O A:THR200 4.3 10.3 1.0
O09 A:FBT555 4.4 11.3 1.0
CA A:THR199 4.4 9.8 1.0
C A:THR200 4.5 11.4 1.0
C A:LEU198 4.5 11.6 1.0
ZN A:ZN262 4.6 21.4 1.0
CA A:LEU198 4.6 11.6 1.0
F12 A:FBT555 4.9 21.6 1.0
CB A:THR199 4.9 11.4 1.0
NE2 A:HIS94 5.0 16.9 1.0

Fluorine binding site 2 out of 2 in 1if5

Go back to Fluorine Binding Sites List in 1if5
Fluorine binding site 2 out of 2 in the Carbonic Anhydrase II Complexed with 2,6-Difluorobenzenesulfonamide


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Carbonic Anhydrase II Complexed with 2,6-Difluorobenzenesulfonamide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F555

b:21.6
occ:1.00
F12 A:FBT555 0.0 21.6 1.0
C05 A:FBT555 1.4 11.5 1.0
C06 A:FBT555 2.4 16.1 1.0
O09 A:FBT555 2.4 11.3 1.0
C04 A:FBT555 2.4 13.3 1.0
CG2 A:VAL121 2.8 6.8 1.0
S07 A:FBT555 2.9 10.3 1.0
CG1 A:VAL121 3.4 9.2 1.0
CE1 A:HIS94 3.6 13.8 1.0
CB A:VAL121 3.7 7.8 1.0
C01 A:FBT555 3.7 14.7 1.0
C03 A:FBT555 3.7 14.0 1.0
O08 A:FBT555 3.8 10.5 1.0
CG2 A:VAL143 4.0 6.0 1.0
NP0 A:FBT555 4.1 12.9 1.0
C02 A:FBT555 4.2 14.9 1.0
NE2 A:HIS94 4.4 16.9 1.0
CG1 A:VAL143 4.6 5.8 1.0
ND1 A:HIS94 4.6 14.7 1.0
CA A:VAL121 4.7 9.8 1.0
F11 A:FBT555 4.9 17.9 1.0
ZN A:ZN262 4.9 21.4 1.0
CB A:VAL143 4.9 6.5 1.0
CD2 A:LEU198 5.0 11.5 1.0

Reference:

C.-Y.Kim, D.W.Christianson. Binding of Fluorine Substituted Benzenesulfonamides to Carbonic Anhydrase II To Be Published.
Page generated: Sun Dec 13 11:30:20 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