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Fluorine in PDB 4y11: Trypsin in Complex with with Bpti Mutant (2S)-2-Amino-4,4,4- Trifluorobutanoic Acid

Enzymatic activity of Trypsin in Complex with with Bpti Mutant (2S)-2-Amino-4,4,4- Trifluorobutanoic Acid

All present enzymatic activity of Trypsin in Complex with with Bpti Mutant (2S)-2-Amino-4,4,4- Trifluorobutanoic Acid:
3.4.21.4;

Protein crystallography data

The structure of Trypsin in Complex with with Bpti Mutant (2S)-2-Amino-4,4,4- Trifluorobutanoic Acid, PDB code: 4y11 was solved by B.Loll, S.Ye, A.A.Berger, U.Muelow, C.Alings, M.C.Wahl, B.Koksch, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.10 / 1.30
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 74.971, 82.102, 123.578, 90.00, 90.00, 90.00
R / Rfree (%) 13.4 / 15.6

Other elements in 4y11:

The structure of Trypsin in Complex with with Bpti Mutant (2S)-2-Amino-4,4,4- Trifluorobutanoic Acid also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Trypsin in Complex with with Bpti Mutant (2S)-2-Amino-4,4,4- Trifluorobutanoic Acid (pdb code 4y11). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Trypsin in Complex with with Bpti Mutant (2S)-2-Amino-4,4,4- Trifluorobutanoic Acid, PDB code: 4y11:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in 4y11

Go back to Fluorine Binding Sites List in 4y11
Fluorine binding site 1 out of 3 in the Trypsin in Complex with with Bpti Mutant (2S)-2-Amino-4,4,4- Trifluorobutanoic Acid


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Trypsin in Complex with with Bpti Mutant (2S)-2-Amino-4,4,4- Trifluorobutanoic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
I:F15

b:14.2
occ:1.00
FAC I:3EG15 0.0 14.2 1.0
CG I:3EG15 1.3 13.2 1.0
FAE I:3EG15 2.1 14.0 1.0
FAD I:3EG15 2.1 14.2 1.0
CB I:3EG15 2.4 12.1 1.0
HA E:TRP213 2.6 15.5 1.0
HBA I:3EG15 2.6 14.5 1.0
CA I:3EG15 3.0 11.2 1.0
HA I:3EG15 3.0 13.5 1.0
N I:3EG15 3.0 11.8 1.0
HB I:3EG15 3.2 14.5 1.0
H I:3EG15 3.2 14.2 1.0
O I:PRO13 3.3 13.2 1.0
CA E:TRP213 3.4 12.9 1.0
O I:HOH237 3.4 17.6 1.0
C I:CYS14 3.4 11.8 1.0
O E:HOH431 3.4 20.4 1.0
C E:TRP213 3.5 13.5 1.0
H E:GLY214 3.6 16.8 1.0
HA I:CYS14 3.6 14.4 1.0
N E:GLY214 3.6 14.0 1.0
O E:SER212 3.7 12.8 1.0
N E:TRP213 3.9 12.9 1.0
O I:CYS14 3.9 12.5 1.0
O E:HOH537 3.9 20.3 1.0
C E:SER212 4.1 12.3 1.0
CA I:CYS14 4.1 12.0 1.0
HE22 E:GLN194 4.1 18.6 1.0
O E:TRP213 4.1 14.5 1.0
HE21 E:GLN194 4.2 18.6 1.0
C I:PRO13 4.3 12.7 1.0
NE2 E:GLN194 4.3 15.5 1.0
O E:HOH538 4.3 18.1 1.0
HA3 E:GLY214 4.3 18.5 1.0
HG12 E:VAL211 4.4 15.8 1.0
H E:TRP213 4.5 15.5 1.0
C I:3EG15 4.5 11.7 1.0
HA E:CYS193 4.5 15.1 1.0
CA E:GLY214 4.6 15.4 1.0
CB E:TRP213 4.6 13.3 1.0
HB2 E:TRP213 4.6 16.0 1.0
N I:CYS14 4.7 12.6 1.0
OG E:SER197 4.7 12.2 1.0
HB3 E:TRP213 4.8 16.0 1.0
HG13 E:VAL211 4.8 15.8 1.0
HG E:SER197 4.8 14.7 1.0
CG1 E:VAL211 5.0 13.2 1.0
HB2 E:SER192 5.0 18.1 0.3

Fluorine binding site 2 out of 3 in 4y11

Go back to Fluorine Binding Sites List in 4y11
Fluorine binding site 2 out of 3 in the Trypsin in Complex with with Bpti Mutant (2S)-2-Amino-4,4,4- Trifluorobutanoic Acid


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Trypsin in Complex with with Bpti Mutant (2S)-2-Amino-4,4,4- Trifluorobutanoic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
I:F15

b:14.2
occ:1.00
FAD I:3EG15 0.0 14.2 1.0
CG I:3EG15 1.3 13.2 1.0
FAC I:3EG15 2.1 14.2 1.0
FAE I:3EG15 2.1 14.0 1.0
CB I:3EG15 2.3 12.1 1.0
HB I:3EG15 2.5 14.5 1.0
HBA I:3EG15 2.6 14.5 1.0
HB3 E:SER192 3.0 18.1 0.3
HB2 E:SER192 3.1 18.1 0.3
O E:HOH537 3.1 20.3 1.0
OG E:SER192 3.3 14.9 0.7
HG13 E:VAL211 3.3 15.8 1.0
HB2 E:SER192 3.4 17.5 0.7
HG12 E:VAL211 3.4 15.8 1.0
HA E:CYS193 3.4 15.1 1.0
CB E:SER192 3.5 15.1 0.3
HG11 E:VAL211 3.5 15.8 1.0
O E:HOH431 3.5 20.4 1.0
C E:SER192 3.6 14.3 1.0
N E:CYS193 3.6 13.2 1.0
CG1 E:VAL211 3.6 13.2 1.0
O E:HOH538 3.6 18.1 1.0
O E:SER192 3.6 15.3 1.0
CA I:3EG15 3.7 11.2 1.0
CB E:SER192 3.8 14.6 0.7
HA I:3EG15 3.8 13.5 1.0
CA E:CYS193 3.8 12.6 1.0
O E:CYS193 3.8 13.1 1.0
H E:CYS193 3.9 15.9 1.0
C E:CYS193 3.9 12.8 1.0
HG E:SER192 4.0 17.9 0.7
HB2 E:ASP196 4.1 14.7 1.0
CA E:SER192 4.2 14.4 0.3
CA E:SER192 4.3 13.8 0.7
HA E:TRP213 4.3 15.5 1.0
N I:3EG15 4.4 11.8 1.0
H I:3EG15 4.5 14.2 1.0
OG E:SER192 4.6 15.0 0.3
HB3 E:SER192 4.7 17.5 0.7
C E:TRP213 4.7 13.5 1.0
N E:GLN194 4.7 13.2 1.0
C I:3EG15 4.8 11.7 1.0
O I:3EG15 4.8 11.9 1.0
O I:HOH237 4.8 17.6 1.0
O E:TRP213 4.8 14.5 1.0
HA E:SER192 4.8 17.3 0.3
CA E:TRP213 4.9 12.9 1.0
O E:SER212 4.9 12.8 1.0
N E:TRP213 4.9 12.9 1.0
HA E:GLN194 4.9 15.4 1.0
HA E:SER192 5.0 16.5 0.7
C E:SER212 5.0 12.3 1.0
OG E:SER197 5.0 12.2 1.0
H E:SER212 5.0 15.2 1.0

Fluorine binding site 3 out of 3 in 4y11

Go back to Fluorine Binding Sites List in 4y11
Fluorine binding site 3 out of 3 in the Trypsin in Complex with with Bpti Mutant (2S)-2-Amino-4,4,4- Trifluorobutanoic Acid


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Trypsin in Complex with with Bpti Mutant (2S)-2-Amino-4,4,4- Trifluorobutanoic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
I:F15

b:14.0
occ:1.00
FAE I:3EG15 0.0 14.0 1.0
CG I:3EG15 1.3 13.2 1.0
FAC I:3EG15 2.1 14.2 1.0
FAD I:3EG15 2.1 14.2 1.0
CB I:3EG15 2.4 12.1 1.0
HA I:3EG15 2.4 13.5 1.0
HB I:3EG15 2.6 14.5 1.0
HA E:CYS193 2.6 15.1 1.0
CA I:3EG15 2.9 11.2 1.0
C E:CYS193 3.1 12.8 1.0
HE22 E:GLN194 3.2 18.6 1.0
HBA I:3EG15 3.2 14.5 1.0
O E:HOH431 3.2 20.4 1.0
CA E:CYS193 3.2 12.6 1.0
NE2 E:GLN194 3.3 15.5 1.0
N E:GLN194 3.3 13.2 1.0
O E:CYS193 3.4 13.1 1.0
HA E:GLN194 3.5 15.4 1.0
HE21 E:GLN194 3.5 18.6 1.0
O I:HOH237 3.5 17.6 1.0
H E:GLN194 3.5 15.8 1.0
CD E:GLN194 3.7 15.2 1.0
N I:3EG15 3.7 11.8 1.0
N E:CYS193 3.9 13.2 1.0
CA E:GLN194 3.9 12.9 1.0
OE1 E:GLN194 4.0 16.4 1.0
C I:3EG15 4.1 11.7 1.0
O I:CYS14 4.1 12.5 1.0
O E:SER192 4.1 15.3 1.0
C I:CYS14 4.2 11.8 1.0
H I:3EG15 4.2 14.2 1.0
C E:SER192 4.3 14.3 1.0
O I:3EG15 4.3 11.9 1.0
HG3 E:GLN194 4.3 17.8 1.0
H E:CYS193 4.3 15.9 1.0
O E:HOH537 4.4 20.3 1.0
CG E:GLN194 4.4 14.9 1.0
SG E:CYS217 4.5 19.9 1.0
CB E:CYS193 4.5 15.4 1.0
O I:PRO13 4.6 13.2 1.0
HB3 E:SER192 4.7 18.1 0.3
HA E:TRP213 4.7 15.5 1.0
CB E:GLN194 4.7 13.5 1.0
HB2 E:SER192 4.9 18.1 0.3
HB2 E:ASP196 4.9 14.7 1.0
SG E:CYS193 5.0 17.7 1.0
HB2 E:SER192 5.0 17.5 0.7

Reference:

S.Ye, B.Loll, A.A.Berger, U.Mulow, C.Alings, M.C.Wahl, B.Koksch. Fluorine Teams Up with Water to Restore Inhibitor Activity to Mutant Bpti. Chem Sci V. 6 5246 2015.
ISSN: ISSN 2041-6520
PubMed: 29449928
DOI: 10.1039/C4SC03227F
Page generated: Tue Jul 15 01:36:07 2025

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