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Fluorine in PDB 1b0f: Crystal Structure of Human Neutrophil Elastase with Mdl 101, 146

Enzymatic activity of Crystal Structure of Human Neutrophil Elastase with Mdl 101, 146

All present enzymatic activity of Crystal Structure of Human Neutrophil Elastase with Mdl 101, 146:
3.4.21.37;

Protein crystallography data

The structure of Crystal Structure of Human Neutrophil Elastase with Mdl 101, 146, PDB code: 1b0f was solved by H.A.Schreuder, W.A.Metz, N.P.Peet, J.T.Pelton, C.Tardif, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 3.00
Space group P 43 2 2
Cell size a, b, c (Å), α, β, γ (°) 75.800, 75.800, 108.500, 90.00, 90.00, 90.00
R / Rfree (%) 16 / n/a

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of Human Neutrophil Elastase with Mdl 101, 146 (pdb code 1b0f). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 5 binding sites of Fluorine where determined in the Crystal Structure of Human Neutrophil Elastase with Mdl 101, 146, PDB code: 1b0f:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5;

Fluorine binding site 1 out of 5 in 1b0f

Go back to Fluorine Binding Sites List in 1b0f
Fluorine binding site 1 out of 5 in the Crystal Structure of Human Neutrophil Elastase with Mdl 101, 146


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 Human Neutrophil Elastase with Mdl 101, 146 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F300

b:10.1
occ:1.00
 F75 A:SEI300 0.0 10.1 1.0
C73 A:SEI300 1.4 18.7 1.0
C77 A:SEI300 2.2 16.1 1.0
F80 A:SEI300 2.3 19.1 1.0
F76 A:SEI300 2.3 10.6 1.0
CB A:SER195 2.6 2.0 1.0
F79 A:SEI300 2.7 24.2 1.0
C71 A:SEI300 2.7 15.2 1.0
OG A:SER195 2.8 17.4 1.0
SG A:CYS42 3.0 2.9 1.0
NE2 A:HIS57 3.0 2.2 1.0
O74 A:SEI300 3.3 12.9 1.0
F78 A:SEI300 3.4 12.0 1.0
CD2 A:HIS57 3.5 2.0 1.0
SG A:CYS58 3.7 3.0 1.0
O A:HOH426 3.8 54.6 1.0
C59 A:SEI300 4.0 9.3 1.0
CA A:SER195 4.0 2.0 1.0
O A:PHE41 4.2 5.8 1.0
CE1 A:HIS57 4.2 2.0 1.0
N53 A:SEI300 4.3 16.2 1.0
N A:SER195 4.4 4.1 1.0
O A:SER195 4.5 2.0 1.0
C A:SER195 4.6 3.5 1.0
CG A:HIS57 4.7 2.0 1.0
CB A:CYS42 4.7 2.4 1.0
C52 A:SEI300 4.9 10.1 1.0
CA A:CYS58 4.9 4.8 1.0
CB A:CYS58 4.9 3.5 1.0

Fluorine binding site 2 out of 5 in 1b0f

Go back to Fluorine Binding Sites List in 1b0f
Fluorine binding site 2 out of 5 in the Crystal Structure of Human Neutrophil Elastase with Mdl 101, 146


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 Human Neutrophil Elastase with Mdl 101, 146 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F300

b:10.6
occ:1.00
 F76 A:SEI300 0.0 10.6 1.0
C73 A:SEI300 1.4 18.7 1.0
C77 A:SEI300 2.3 16.1 1.0
F75 A:SEI300 2.3 10.1 1.0
C71 A:SEI300 2.4 15.2 1.0
F78 A:SEI300 2.5 12.0 1.0
N53 A:SEI300 2.6 16.2 1.0
F80 A:SEI300 2.7 19.1 1.0
C52 A:SEI300 2.7 10.1 1.0
C59 A:SEI300 2.7 9.3 1.0
NE2 A:HIS57 2.8 2.2 1.0
OG A:SER195 2.8 17.4 1.0
O58 A:SEI300 2.9 18.6 1.0
CD2 A:HIS57 3.2 2.0 1.0
C47 A:SEI300 3.4 7.1 1.0
F79 A:SEI300 3.4 24.2 1.0
C44 A:SEI300 3.6 3.9 1.0
O74 A:SEI300 3.6 12.9 1.0
CB A:SER195 3.7 2.0 1.0
O A:HOH426 3.7 54.6 1.0
CE1 A:HIS57 3.9 2.0 1.0
C61 A:SEI300 4.2 8.4 1.0
CG A:HIS57 4.5 2.0 1.0
C46 A:SEI300 4.5 4.0 1.0
O A:SER214 4.7 5.2 1.0
N54 A:SEI300 4.7 2.0 1.0
ND1 A:HIS57 4.8 5.4 1.0
C62 A:SEI300 4.8 2.0 1.0

Fluorine binding site 3 out of 5 in 1b0f

Go back to Fluorine Binding Sites List in 1b0f
Fluorine binding site 3 out of 5 in the Crystal Structure of Human Neutrophil Elastase with Mdl 101, 146


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 Human Neutrophil Elastase with Mdl 101, 146 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F300

b:12.0
occ:1.00
 F78 A:SEI300 0.0 12.0 1.0
C77 A:SEI300 1.3 16.1 1.0
F79 A:SEI300 2.2 24.2 1.0
C73 A:SEI300 2.2 18.7 1.0
F80 A:SEI300 2.2 19.1 1.0
F76 A:SEI300 2.5 10.6 1.0
C71 A:SEI300 2.7 15.2 1.0
C59 A:SEI300 3.1 9.3 1.0
F75 A:SEI300 3.4 10.1 1.0
O74 A:SEI300 3.4 12.9 1.0
O58 A:SEI300 3.4 18.6 1.0
CD1 A:PHE192 3.7 13.7 1.0
N53 A:SEI300 3.8 16.2 1.0
N A:GLY193 3.8 2.0 1.0
C52 A:SEI300 3.9 10.1 1.0
CB A:PHE192 3.9 2.0 1.0
CA A:PHE192 4.0 2.0 1.0
OG A:SER195 4.1 17.4 1.0
CG A:PHE192 4.3 3.5 1.0
C61 A:SEI300 4.3 8.4 1.0
C A:PHE192 4.4 2.2 1.0
CE1 A:PHE192 4.7 17.9 1.0
O A:HOH426 4.7 54.6 1.0
CA A:GLY193 4.8 2.0 1.0
CB A:SER195 5.0 2.0 1.0
C66 A:SEI300 5.0 12.8 1.0

Fluorine binding site 4 out of 5 in 1b0f

Go back to Fluorine Binding Sites List in 1b0f
Fluorine binding site 4 out of 5 in the Crystal Structure of Human Neutrophil Elastase with Mdl 101, 146


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 Human Neutrophil Elastase with Mdl 101, 146 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F300

b:24.2
occ:1.00
 F79 A:SEI300 0.0 24.2 1.0
C77 A:SEI300 1.3 16.1 1.0
F80 A:SEI300 2.2 19.1 1.0
F78 A:SEI300 2.2 12.0 1.0
C73 A:SEI300 2.3 18.7 1.0
F75 A:SEI300 2.7 10.1 1.0
C71 A:SEI300 2.7 15.2 1.0
O74 A:SEI300 2.7 12.9 1.0
N A:GLY193 2.9 2.0 1.0
CA A:GLY193 3.2 2.0 1.0
O A:PHE41 3.4 5.8 1.0
F76 A:SEI300 3.4 10.6 1.0
OG A:SER195 3.8 17.4 1.0
C A:PHE192 3.9 2.2 1.0
C59 A:SEI300 3.9 9.3 1.0
C A:GLY193 4.0 3.6 1.0
CB A:SER195 4.2 2.0 1.0
CA A:PHE192 4.3 2.0 1.0
SG A:CYS42 4.4 2.9 1.0
N A:ASP194 4.4 6.3 1.0
N A:SER195 4.6 4.1 1.0
C A:PHE41 4.6 3.8 1.0
CB A:PHE192 4.7 2.0 1.0
O A:GLY193 4.8 6.2 1.0
O A:PHE192 4.9 4.4 1.0
C61 A:SEI300 4.9 8.4 1.0
N53 A:SEI300 4.9 16.2 1.0

Fluorine binding site 5 out of 5 in 1b0f

Go back to Fluorine Binding Sites List in 1b0f
Fluorine binding site 5 out of 5 in the Crystal Structure of Human Neutrophil Elastase with Mdl 101, 146


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 Human Neutrophil Elastase with Mdl 101, 146 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F300

b:19.1
occ:1.00
 F80 A:SEI300 0.0 19.1 1.0
C77 A:SEI300 1.3 16.1 1.0
F79 A:SEI300 2.2 24.2 1.0
F78 A:SEI300 2.2 12.0 1.0
C73 A:SEI300 2.2 18.7 1.0
F75 A:SEI300 2.3 10.1 1.0
F76 A:SEI300 2.7 10.6 1.0
O A:HOH426 3.1 54.6 1.0
C71 A:SEI300 3.6 15.2 1.0
O A:PHE41 4.1 5.8 1.0
O74 A:SEI300 4.3 12.9 1.0
SG A:CYS42 4.4 2.9 1.0
OG A:SER195 4.5 17.4 1.0
C59 A:SEI300 4.5 9.3 1.0
CD2 A:HIS57 4.6 2.0 1.0
NE2 A:HIS57 4.7 2.2 1.0
CB A:SER195 4.8 2.0 1.0
O58 A:SEI300 4.9 18.6 1.0
N A:GLY193 4.9 2.0 1.0

Reference:

R.J.Cregge, S.L.Durham, R.A.Farr, S.L.Gallion, C.M.Hare, R.V.Hoffman, M.J.Janusz, H.O.Kim, J.R.Koehl, S.Mehdi, W.A.Metz, N.P.Peet, J.T.Pelton, H.A.Schreuder, S.Sunder, C.Tardif. Inhibition of Human Neutrophil Elastase. 4. Design, Synthesis, X-Ray Crystallographic Analysis, and Structure-Activity Relationships For A Series of P2-Modified, Orally Active Peptidyl Pentafluoroethyl Ketones. J.Med.Chem. V. 41 2461 1998.
ISSN: ISSN 0022-2623
PubMed: 9651152
DOI: 10.1021/JM970812E
Page generated: Wed Jul 31 10:50:17 2024

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