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Chlorine in PDB 1gj4: Selectivity at S1, H2O Displacement, Upa, Tpa, SER190/ALA190 Protease, Structure-Based Drug Design

Enzymatic activity of Selectivity at S1, H2O Displacement, Upa, Tpa, SER190/ALA190 Protease, Structure-Based Drug Design

All present enzymatic activity of Selectivity at S1, H2O Displacement, Upa, Tpa, SER190/ALA190 Protease, Structure-Based Drug Design:
3.4.21.5;

Protein crystallography data

The structure of Selectivity at S1, H2O Displacement, Upa, Tpa, SER190/ALA190 Protease, Structure-Based Drug Design, PDB code: 1gj4 was solved by B.A.Katz, P.A.Sprengeler, C.Luong, E.Verner, J.R.Spencer, J.G.Breitenbucher, H.Hui, D.Mcgee, D.Allen, A.Martelli, R.L.Mackman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 7.00 / 1.81
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 71.370, 72.090, 72.840, 90.00, 100.97, 90.00
R / Rfree (%) 20.2 / 23.6

Other elements in 1gj4:

The structure of Selectivity at S1, H2O Displacement, Upa, Tpa, SER190/ALA190 Protease, Structure-Based Drug Design also contains other interesting chemical elements:

Sodium (Na) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Selectivity at S1, H2O Displacement, Upa, Tpa, SER190/ALA190 Protease, Structure-Based Drug Design (pdb code 1gj4). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Selectivity at S1, H2O Displacement, Upa, Tpa, SER190/ALA190 Protease, Structure-Based Drug Design, PDB code: 1gj4:

Chlorine binding site 1 out of 1 in 1gj4

Go back to Chlorine Binding Sites List in 1gj4
Chlorine binding site 1 out of 1 in the Selectivity at S1, H2O Displacement, Upa, Tpa, SER190/ALA190 Protease, Structure-Based Drug Design


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Selectivity at S1, H2O Displacement, Upa, Tpa, SER190/ALA190 Protease, Structure-Based Drug Design within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Cl410

b:36.1
occ:0.84
CL2 H:132410 0.0 36.1 0.8
C2 H:132410 1.8 26.9 0.8
HH21 H:132410 1.8 19.0 0.8
HG11 H:VAL213 2.5 20.2 1.0
N2 H:132410 2.7 17.9 0.8
HB2 H:ALA190 2.7 16.4 1.0
C3 H:132410 2.8 29.2 0.8
C1 H:132410 2.8 24.4 0.8
HC3 H:132410 2.9 29.6 0.8
HG12 H:VAL213 3.1 20.9 1.0
C7 H:132410 3.2 27.8 0.8
CG1 H:VAL213 3.3 19.4 1.0
HH22 H:132410 3.5 20.3 0.8
HA3 H:GLY226 3.6 13.3 1.0
CB H:ALA190 3.7 15.4 1.0
H H:PHE227 3.7 10.5 1.0
HH H:TYR228 3.7 7.8 1.0
HG13 H:VAL213 3.7 21.9 1.0
H H:SER214 3.8 17.1 1.0
O H:TRP215 3.8 30.2 1.0
HB3 H:ALA190 3.8 16.9 1.0
HA2 H:GLY226 3.9 15.8 1.0
H H:TRP215 4.0 26.6 1.0
C H:TRP215 4.0 23.4 1.0
HA H:VAL213 4.0 17.8 1.0
C4 H:132410 4.1 29.2 0.8
O H:PHE227 4.1 15.0 1.0
N H:TRP215 4.1 27.2 1.0
HB1 H:ALA190 4.1 17.6 1.0
C6 H:132410 4.1 29.6 0.8
HA H:TRP215 4.1 24.2 1.0
CA H:GLY226 4.1 12.3 1.0
N H:SER214 4.3 15.8 1.0
CA H:TRP215 4.3 21.1 1.0
H H:ALA190 4.4 17.5 1.0
N H:PHE227 4.4 9.1 1.0
HA3 H:GLY216 4.4 23.7 1.0
CB H:VAL213 4.5 19.6 1.0
N1 H:132410 4.5 29.8 0.8
CA H:VAL213 4.5 14.6 1.0
C H:SER214 4.6 21.3 1.0
C5 H:132410 4.6 28.7 0.8
N H:GLY216 4.6 19.7 1.0
OH H:TYR228 4.6 11.4 1.0
CZ H:TYR228 4.6 2.9 1.0
HG23 H:VAL213 4.6 20.8 1.0
CE2 H:TYR228 4.7 8.4 1.0
C H:VAL213 4.7 15.8 1.0
C H:GLY226 4.7 10.8 1.0
HE2 H:TYR228 4.8 8.2 1.0
CA H:ALA190 4.8 18.7 1.0
OD1 H:ASP189 4.9 24.4 1.0
C H:ALA190 5.0 22.2 1.0
N H:ALA190 5.0 17.9 1.0

Reference:

B.A.Katz, P.A.Sprengeler, C.Luong, E.Verner, K.Elrod, M.Kirtley, J.Janc, J.R.Spencer, J.G.Breitenbucher, H.Hui, D.Mcgee, D.Allen, A.Martelli, R.L.Mackman. Engineering Inhibitors Highly Selective For the S1 Sites of SER190 Trypsin-Like Serine Protease Drug Targets. Chem.Biol. V. 8 1107 2001.
ISSN: ISSN 1074-5521
PubMed: 11731301
DOI: 10.1016/S1074-5521(01)00084-9
Page generated: Fri Jul 19 22:11:05 2024

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