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Fluorine in PDB 4jqg: Crystal Structure of An Inactive Mutant of Mmp-9 Catalytic Domain in Complex with A Fluorogenic Synthetic Peptidic Substrate with A Fluorine Atom.

Enzymatic activity of Crystal Structure of An Inactive Mutant of Mmp-9 Catalytic Domain in Complex with A Fluorogenic Synthetic Peptidic Substrate with A Fluorine Atom.

All present enzymatic activity of Crystal Structure of An Inactive Mutant of Mmp-9 Catalytic Domain in Complex with A Fluorogenic Synthetic Peptidic Substrate with A Fluorine Atom.:
3.4.24.35;

Protein crystallography data

The structure of Crystal Structure of An Inactive Mutant of Mmp-9 Catalytic Domain in Complex with A Fluorogenic Synthetic Peptidic Substrate with A Fluorine Atom., PDB code: 4jqg was solved by E.A.Stura, L.Vera, E.Cassar-Lajeunesse, I.Tranchant, M.Amoura, V.Dive, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.52 / 1.85
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 34.140, 57.480, 171.420, 90.00, 90.00, 90.00
R / Rfree (%) 19.3 / 24.2

Other elements in 4jqg:

The structure of Crystal Structure of An Inactive Mutant of Mmp-9 Catalytic Domain in Complex with A Fluorogenic Synthetic Peptidic Substrate with A Fluorine Atom. also contains other interesting chemical elements:

Strontium (Sr) 3 atoms
Zinc (Zn) 4 atoms
Calcium (Ca) 3 atoms
Sodium (Na) 3 atoms

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of An Inactive Mutant of Mmp-9 Catalytic Domain in Complex with A Fluorogenic Synthetic Peptidic Substrate with A Fluorine Atom. (pdb code 4jqg). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Crystal Structure of An Inactive Mutant of Mmp-9 Catalytic Domain in Complex with A Fluorogenic Synthetic Peptidic Substrate with A Fluorine Atom., PDB code: 4jqg:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in 4jqg

Go back to Fluorine Binding Sites List in 4jqg
Fluorine binding site 1 out of 2 in the Crystal Structure of An Inactive Mutant of Mmp-9 Catalytic Domain in Complex with A Fluorogenic Synthetic Peptidic Substrate with A Fluorine Atom.


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 An Inactive Mutant of Mmp-9 Catalytic Domain in Complex with A Fluorogenic Synthetic Peptidic Substrate with A Fluorine Atom. within 5.0Å range:
probe atom residue distance (Å) B Occ
P:F5

b:18.0
occ:1.00
F P:PFF5 0.0 18.0 1.0
CZ P:PFF5 1.3 18.8 1.0
CE2 P:PFF5 2.4 14.7 1.0
CE1 P:PFF5 2.4 13.7 1.0
O2 A:EDO309 2.9 24.7 1.0
O A:HOH446 3.2 26.0 1.0
C2 A:EDO309 3.2 24.1 1.0
CD2 P:PFF5 3.6 11.9 1.0
CD1 P:PFF5 3.6 14.7 1.0
CA A:TYR248 3.6 19.5 1.0
O A:MET247 4.0 18.2 1.0
CD1 A:TYR248 4.0 20.4 1.0
CG P:PFF5 4.1 20.1 1.0
CB A:TYR248 4.2 18.8 1.0
N A:TYR248 4.2 13.7 1.0
O A:LEU243 4.2 16.9 1.0
ND1 A:HIS226 4.3 13.6 1.0
CB A:HIS226 4.3 9.6 1.0
C A:MET247 4.3 16.5 1.0
O A:TYR245 4.4 15.3 1.0
CG A:HIS226 4.4 16.9 1.0
O1 A:EDO309 4.4 27.6 1.0
C1 A:EDO309 4.5 31.3 1.0
CG A:TYR248 4.5 17.0 1.0
N A:ARG249 4.5 19.7 1.0
C A:TYR248 4.7 17.2 1.0
O A:LEU222 4.9 9.9 1.0
CE1 A:TYR248 4.9 17.9 1.0
CE1 A:HIS226 5.0 11.8 1.0

Fluorine binding site 2 out of 2 in 4jqg

Go back to Fluorine Binding Sites List in 4jqg
Fluorine binding site 2 out of 2 in the Crystal Structure of An Inactive Mutant of Mmp-9 Catalytic Domain in Complex with A Fluorogenic Synthetic Peptidic Substrate with A Fluorine Atom.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of An Inactive Mutant of Mmp-9 Catalytic Domain in Complex with A Fluorogenic Synthetic Peptidic Substrate with A Fluorine Atom. within 5.0Å range:
probe atom residue distance (Å) B Occ
Q:F5

b:20.2
occ:1.00
F Q:PFF5 0.0 20.2 1.0
CZ Q:PFF5 1.4 22.4 1.0
CE1 Q:PFF5 2.4 20.7 1.0
CE2 Q:PFF5 2.4 17.6 1.0
O B:HOH434 3.1 24.1 1.0
O B:HOH584 3.2 28.8 1.0
O B:HOH510 3.2 30.1 1.0
CA B:TYR248 3.5 24.9 1.0
CD1 Q:PFF5 3.6 18.0 1.0
CD2 Q:PFF5 3.7 21.3 1.0
CD1 B:TYR248 3.9 25.9 1.0
O B:MET247 3.9 22.6 1.0
CB B:TYR248 4.0 25.7 1.0
N B:TYR248 4.1 19.9 1.0
CG Q:PFF5 4.1 18.8 1.0
C B:MET247 4.3 21.1 1.0
ND1 B:HIS226 4.3 14.8 1.0
CG B:TYR248 4.3 21.5 1.0
CB B:HIS226 4.3 11.0 1.0
N B:ARG249 4.3 26.1 0.5
N B:ARG249 4.4 26.1 0.6
CG B:HIS226 4.4 13.8 1.0
O B:LEU243 4.4 14.5 1.0
NA B:NA310 4.4 35.4 1.0
O B:TYR245 4.4 15.9 1.0
C B:TYR248 4.5 28.8 1.0
CE1 B:TYR248 4.9 23.1 1.0
O B:LEU222 4.9 12.9 1.0
CE1 B:HIS226 5.0 14.3 1.0

Reference:

I.Tranchant, L.Vera, B.Czarny, M.Amoura, E.Cassar, F.Beau, E.A.Stura, V.Dive. Halogen Bonding Controls Selectivity of Fret Substrate Probes For Mmp-9. Chem.Biol. V. 21 408 2014.
ISSN: ISSN 1074-5521
PubMed: 24583051
DOI: 10.1016/J.CHEMBIOL.2014.01.008
Page generated: Mon Jul 14 22:39:43 2025

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