Fluorine in PDB 7ph1: Trypsin in Complex with Bpti Mutant (2S)-2-Amino-4-Monofluorobutanoic Acid

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

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

Protein crystallography data

The structure of Trypsin in Complex with Bpti Mutant (2S)-2-Amino-4-Monofluorobutanoic Acid, PDB code: 7ph1 was solved by N.Dimos, J.Leppkes, B.Koksch, B.Loll, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.56 / 1.18
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 74.975, 81.289, 124.248, 90, 90, 90
R / Rfree (%) 14.9 / 16.6

Other elements in 7ph1:

The structure of Trypsin in Complex with Bpti Mutant (2S)-2-Amino-4-Monofluorobutanoic 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 Bpti Mutant (2S)-2-Amino-4-Monofluorobutanoic Acid (pdb code 7ph1). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Trypsin in Complex with Bpti Mutant (2S)-2-Amino-4-Monofluorobutanoic Acid, PDB code: 7ph1:

Fluorine binding site 1 out of 1 in 7ph1

Go back to Fluorine Binding Sites List in 7ph1
Fluorine binding site 1 out of 1 in the Trypsin in Complex with Bpti Mutant (2S)-2-Amino-4-Monofluorobutanoic 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 Bpti Mutant (2S)-2-Amino-4-Monofluorobutanoic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
I:F15

b:18.2
occ:1.00
 FAE I:7OZ15 0.0 18.2 1.0
CG I:7OZ15 1.4 16.3 1.0
HG3 I:7OZ15 2.0 19.6 1.0
HG2 I:7OZ15 2.0 19.6 1.0
CB I:7OZ15 2.4 14.9 1.0
HA I:7OZ15 2.5 16.9 1.0
HB2 I:7OZ15 2.5 17.8 1.0
HA E:CYS193 2.6 17.4 1.0
O E:HOH467 3.0 23.3 1.0
CA I:7OZ15 3.0 14.1 1.0
C E:CYS193 3.2 14.8 1.0
CA E:CYS193 3.2 14.5 1.0
O I:HOH246 3.3 17.7 1.0
HE22 E:GLN194 3.3 20.3 1.0
HB3 I:7OZ15 3.3 17.8 1.0
NE2 E:GLN194 3.4 16.9 1.0
N E:GLN194 3.6 14.5 1.0
HE21 E:GLN194 3.6 20.3 1.0
O E:CYS193 3.6 15.6 1.0
HA E:GLN194 3.7 17.4 1.0
N E:CYS193 3.7 15.1 1.0
N I:7OZ15 3.8 14.6 1.0
H E:GLN194 3.8 17.4 1.0
CD E:GLN194 3.9 16.4 1.0
O E:SER192 4.0 16.2 1.0
C E:SER192 4.1 15.8 1.0
O E:HOH550 4.1 22.6 1.0
H E:CYS193 4.2 18.1 1.0
CA E:GLN194 4.2 14.5 1.0
C I:7OZ15 4.2 13.4 1.0
C I:CYS14 4.2 13.9 1.0
H I:7OZ15 4.3 17.5 1.0
O I:CYS14 4.3 14.5 1.0
OE1 E:GLN194 4.3 16.8 1.0
HB3 E:SER192 4.3 19.8 0.6
O I:7OZ15 4.4 13.8 1.0
O I:PRO13 4.5 14.9 1.0
HB2 E:SER192 4.5 19.8 0.6
HA E:TRP213 4.5 17.8 1.0
SG E:CYS217 4.5 19.2 1.0
HG3 E:GLN194 4.6 19.6 1.0
CB E:CYS193 4.6 16.5 1.0
HB2 E:SER192 4.7 19.7 0.4
CG E:GLN194 4.8 16.3 1.0
CB E:SER192 4.8 16.5 0.6
HB2 E:ASP196 4.8 17.3 1.0
HG12 E:VAL211 4.9 17.6 1.0
H E:GLY214 4.9 19.1 1.0
OG E:SER192 4.9 16.6 0.4
HB2 E:CYS193 5.0 19.8 1.0

Reference:

L.Wehrhan, J.Leppkes, N.Dimos, B.Loll, B.Koksch, B.G.Keller. Water Network in the Binding Pocket of Fluorinated Bpti-Trypsin Complexes─Insights From Simulation and Experiment. J.Phys.Chem.B V. 126 9985 2022.
ISSN: ISSN 1089-5647
PubMed: 36409613
DOI: 10.1021/ACS.JPCB.2C05496
Page generated: Fri Aug 2 10:59:27 2024

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