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Fluorine in PDB 1gg6: Crystal Structure of Gamma Chymotrypsin with N-Acetyl-Phenylalanine Trifluoromethyl Ketone Bound at the Active Site

Enzymatic activity of Crystal Structure of Gamma Chymotrypsin with N-Acetyl-Phenylalanine Trifluoromethyl Ketone Bound at the Active Site

All present enzymatic activity of Crystal Structure of Gamma Chymotrypsin with N-Acetyl-Phenylalanine Trifluoromethyl Ketone Bound at the Active Site:
3.4.21.1;

Protein crystallography data

The structure of Crystal Structure of Gamma Chymotrypsin with N-Acetyl-Phenylalanine Trifluoromethyl Ketone Bound at the Active Site, PDB code: 1gg6 was solved by D.Neidhart, Y.Wei, C.Cassidy, J.Lin, W.W.Cleland, P.A.Frey, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 1.40
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 69.190, 69.190, 95.440, 90.00, 90.00, 90.00
R / Rfree (%) 17.5 / 21.2

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of Gamma Chymotrypsin with N-Acetyl-Phenylalanine Trifluoromethyl Ketone Bound at the Active Site (pdb code 1gg6). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 6 binding sites of Fluorine where determined in the Crystal Structure of Gamma Chymotrypsin with N-Acetyl-Phenylalanine Trifluoromethyl Ketone Bound at the Active Site, PDB code: 1gg6:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6;

Fluorine binding site 1 out of 6 in 1gg6

Go back to Fluorine Binding Sites List in 1gg6
Fluorine binding site 1 out of 6 in the Crystal Structure of Gamma Chymotrypsin with N-Acetyl-Phenylalanine Trifluoromethyl Ketone Bound at the Active Site


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 Gamma Chymotrypsin with N-Acetyl-Phenylalanine Trifluoromethyl Ketone Bound at the Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F302

b:25.3
occ:1.00
 F11 B:APL302 0.0 25.3 1.0
C1 B:APL302 1.3 23.3 1.0
F13 B:APL302 2.1 24.1 1.0
F12 B:APL302 2.1 23.7 1.0
C2 B:APL302 2.4 23.0 1.0
OX B:APL302 2.8 24.3 0.5
C3 B:APL302 2.8 21.9 1.0
C4 B:APL302 3.4 19.6 1.0
OY B:APL302 3.5 20.0 0.5
CE B:LYS82 3.6 31.3 1.0
NZ B:LYS82 4.0 32.8 1.0
CG1 B:ILE80 4.1 18.5 1.0
CD1 B:ILE80 4.1 20.1 1.0
N3 B:APL302 4.2 23.2 1.0
CN2 B:APL302 4.4 23.0 1.0
CP1 B:APL302 4.6 18.6 1.0
CP2 B:APL302 4.6 16.3 1.0
CN1 B:APL302 4.7 25.1 1.0
OE2 B:GLU70 4.7 14.9 1.0
O B:HOH492 4.9 13.7 1.0
OE1 B:GLN34 4.9 12.8 1.0
CD B:LYS82 5.0 28.5 1.0

Fluorine binding site 2 out of 6 in 1gg6

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Fluorine binding site 2 out of 6 in the Crystal Structure of Gamma Chymotrypsin with N-Acetyl-Phenylalanine Trifluoromethyl Ketone Bound at the Active Site


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 Gamma Chymotrypsin with N-Acetyl-Phenylalanine Trifluoromethyl Ketone Bound at the Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F302

b:23.7
occ:1.00
 F12 B:APL302 0.0 23.7 1.0
C1 B:APL302 1.3 23.3 1.0
F11 B:APL302 2.1 25.3 1.0
F13 B:APL302 2.2 24.1 1.0
C2 B:APL302 2.4 23.0 1.0
OX B:APL302 2.6 24.3 0.5
OY B:APL302 2.9 20.0 0.5
CG1 B:VAL67 3.2 11.6 1.0
CG2 B:VAL67 3.5 8.8 1.0
OE1 B:GLN34 3.6 12.8 1.0
C3 B:APL302 3.8 21.9 1.0
OE2 B:GLU70 3.8 14.9 1.0
NE2 B:GLN34 3.8 14.1 1.0
OE1 B:GLU70 3.9 16.4 1.0
CB B:VAL67 3.9 8.8 1.0
CG1 B:ILE80 3.9 18.5 1.0
CE B:LYS82 4.0 31.3 1.0
CD B:GLN34 4.1 14.9 1.0
CD B:GLU70 4.1 16.5 1.0
C4 B:APL302 4.4 19.6 1.0
O B:HOH506 4.5 18.3 1.0
CD1 B:ILE80 4.7 20.1 1.0
CB B:ILE80 4.8 15.8 1.0
CG B:LYS82 4.8 25.7 1.0
N3 B:APL302 4.8 23.2 1.0
CG2 B:ILE80 5.0 16.4 1.0

Fluorine binding site 3 out of 6 in 1gg6

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Fluorine binding site 3 out of 6 in the Crystal Structure of Gamma Chymotrypsin with N-Acetyl-Phenylalanine Trifluoromethyl Ketone Bound at the Active Site


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of Gamma Chymotrypsin with N-Acetyl-Phenylalanine Trifluoromethyl Ketone Bound at the Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F302

b:24.1
occ:1.00
 F13 B:APL302 0.0 24.1 1.0
C1 B:APL302 1.3 23.3 1.0
F11 B:APL302 2.1 25.3 1.0
F12 B:APL302 2.2 23.7 1.0
C2 B:APL302 2.4 23.0 1.0
OY B:APL302 2.7 20.0 0.5
OE2 B:GLU70 2.8 14.9 1.0
C4 B:APL302 3.0 19.6 1.0
C3 B:APL302 3.1 21.9 1.0
O B:HOH464 3.4 17.2 1.0
OX B:APL302 3.5 24.3 0.5
CD B:GLU70 3.6 16.5 1.0
CG1 B:ILE80 3.6 18.5 1.0
O B:HOH492 3.7 13.7 1.0
CD1 B:ILE80 3.8 20.1 1.0
CG2 B:ILE80 4.0 16.4 1.0
OE1 B:GLU70 4.1 16.4 1.0
CB B:ILE80 4.3 15.8 1.0
CP1 B:APL302 4.4 18.6 1.0
CG1 B:VAL67 4.4 11.6 1.0
N3 B:APL302 4.4 23.2 1.0
CG B:GLU70 4.6 14.0 1.0
O B:SER75 4.9 12.1 1.0
CP2 B:APL302 5.0 16.3 1.0

Fluorine binding site 4 out of 6 in 1gg6

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Fluorine binding site 4 out of 6 in the Crystal Structure of Gamma Chymotrypsin with N-Acetyl-Phenylalanine Trifluoromethyl Ketone Bound at the Active Site


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Crystal Structure of Gamma Chymotrypsin with N-Acetyl-Phenylalanine Trifluoromethyl Ketone Bound at the Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
C:F301

b:11.5
occ:1.00
 F11 C:APF301 0.0 11.5 1.0
C1 C:APF301 1.3 11.6 1.0
F12 C:APF301 2.2 12.7 1.0
F13 C:APF301 2.2 13.0 1.0
C2 C:APF301 2.4 10.7 1.0
OG C:SER195 2.7 10.1 1.0
CN1 C:APF301 3.0 12.4 1.0
N3 C:APF301 3.0 11.5 1.0
C3 C:APF301 3.1 11.0 1.0
NE2 B:HIS57 3.1 9.5 1.0
ON1 C:APF301 3.2 12.6 1.0
CD2 B:HIS57 3.4 9.3 1.0
O2 C:APF301 3.5 8.6 1.0
CB C:SER195 3.6 9.1 1.0
CN2 C:APF301 3.7 11.5 1.0
CE1 B:HIS57 4.3 9.6 1.0
C4 C:APF301 4.5 11.4 1.0
CG B:HIS57 4.7 8.6 1.0

Fluorine binding site 5 out of 6 in 1gg6

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Fluorine binding site 5 out of 6 in the Crystal Structure of Gamma Chymotrypsin with N-Acetyl-Phenylalanine Trifluoromethyl Ketone Bound at the Active Site


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 5 of Crystal Structure of Gamma Chymotrypsin with N-Acetyl-Phenylalanine Trifluoromethyl Ketone Bound at the Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
C:F301

b:12.7
occ:1.00
 F12 C:APF301 0.0 12.7 1.0
C1 C:APF301 1.3 11.6 1.0
F13 C:APF301 2.1 13.0 1.0
F11 C:APF301 2.2 11.5 1.0
C2 C:APF301 2.4 10.7 1.0
O2 C:APF301 2.7 8.6 1.0
OG C:SER195 2.9 10.1 1.0
CB C:SER195 2.9 9.1 1.0
O B:PHE41 3.7 10.3 1.0
C3 C:APF301 3.8 11.0 1.0
N C:GLY193 3.9 9.5 1.0
SG B:CYS42 4.0 8.8 1.0
NE2 B:HIS57 4.2 9.5 1.0
CA C:SER195 4.3 8.4 1.0
N3 C:APF301 4.4 11.5 1.0
N C:SER195 4.5 9.1 1.0
CA C:GLY193 4.5 8.8 1.0
CD2 B:HIS57 4.7 9.3 1.0
CN1 C:APF301 4.8 12.4 1.0
ON1 C:APF301 4.8 12.6 1.0
C4 C:APF301 4.9 11.4 1.0
C B:PHE41 4.9 10.5 1.0
C C:MET192 4.9 9.5 1.0
CA C:MET192 4.9 10.5 1.0

Fluorine binding site 6 out of 6 in 1gg6

Go back to Fluorine Binding Sites List in 1gg6
Fluorine binding site 6 out of 6 in the Crystal Structure of Gamma Chymotrypsin with N-Acetyl-Phenylalanine Trifluoromethyl Ketone Bound at the Active Site


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 6 of Crystal Structure of Gamma Chymotrypsin with N-Acetyl-Phenylalanine Trifluoromethyl Ketone Bound at the Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
C:F301

b:13.0
occ:1.00
 F13 C:APF301 0.0 13.0 1.0
C1 C:APF301 1.3 11.6 1.0
F12 C:APF301 2.1 12.7 1.0
F11 C:APF301 2.2 11.5 1.0
C2 C:APF301 2.4 10.7 1.0
O2 C:APF301 2.8 8.6 1.0
C3 C:APF301 2.9 11.0 1.0
ON1 C:APF301 3.3 12.6 1.0
CA C:MET192 3.6 10.5 1.0
OG C:SER195 3.6 10.1 1.0
N3 C:APF301 3.6 11.5 1.0
CN1 C:APF301 3.7 12.4 1.0
N C:GLY193 3.7 9.5 1.0
CG C:MET192 3.7 14.6 1.0
CB C:MET192 3.7 11.3 1.0
C C:MET192 4.1 9.5 1.0
C4 C:APF301 4.3 11.4 1.0
CB C:SER195 4.3 9.1 1.0
N C:MET192 4.7 10.8 1.0
CA C:GLY193 4.8 8.8 1.0
CN2 C:APF301 5.0 11.5 1.0

Reference:

D.Neidhart, Y.Wei, C.Cassidy, J.Lin, W.W.Cleland, P.A.Frey. Correlation of Low-Barrier Hydrogen Bonding and Oxyanion Binding in Transition State Analogue Complexes of Chymotrypsin. Biochemistry V. 40 2439 2001.
ISSN: ISSN 0006-2960
PubMed: 11327865
DOI: 10.1021/BI002535A
Page generated: Sun Dec 13 11:29:47 2020

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