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Chlorine in PDB 7mgt: Ftp From Treponema Pallidum Bound to An Adp-Like Inhibitor

Enzymatic activity of Ftp From Treponema Pallidum Bound to An Adp-Like Inhibitor

All present enzymatic activity of Ftp From Treponema Pallidum Bound to An Adp-Like Inhibitor:
2.7.1.180;

Protein crystallography data

The structure of Ftp From Treponema Pallidum Bound to An Adp-Like Inhibitor, PDB code: 7mgt was solved by C.A.Brautigam, R.Deka, M.V.Norgard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.84 / 1.54
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 116.483, 47.106, 57.472, 90, 102.3, 90
R / Rfree (%) 15 / 19.8

Other elements in 7mgt:

The structure of Ftp From Treponema Pallidum Bound to An Adp-Like Inhibitor also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Ftp From Treponema Pallidum Bound to An Adp-Like Inhibitor (pdb code 7mgt). 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 Ftp From Treponema Pallidum Bound to An Adp-Like Inhibitor, PDB code: 7mgt:

Chlorine binding site 1 out of 1 in 7mgt

Go back to Chlorine Binding Sites List in 7mgt
Chlorine binding site 1 out of 1 in the Ftp From Treponema Pallidum Bound to An Adp-Like Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Ftp From Treponema Pallidum Bound to An Adp-Like Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl403

b:21.8
occ:0.50
CL6 A:ZD4403 0.0 21.8 0.5
C2 A:ZD4403 1.8 10.7 1.0
N3 A:ZD4403 2.6 8.7 1.0
H A:ASN98 2.7 14.6 1.0
N1 A:ZD4403 2.7 9.6 1.0
HB3 A:ALA162 2.9 8.3 1.0
O A:ASN98 3.0 14.1 1.0
C A:ASN98 3.1 12.3 1.0
CE1 A:PHE97 3.2 15.1 1.0
HA A:PRO99 3.2 13.1 1.0
N A:ASN98 3.2 12.2 1.0
CD1 A:PHE97 3.2 12.2 1.0
O A:HOH525 3.3 14.3 1.0
O A:HOH614 3.4 15.8 1.0
CZ A:PHE97 3.4 13.8 1.0
N A:PRO99 3.5 12.1 1.0
HE1 A:PHE97 3.5 18.1 1.0
CG A:PHE97 3.5 11.5 1.0
HD1 A:PHE97 3.6 14.6 1.0
CE2 A:PHE97 3.7 11.8 1.0
CB A:ALA162 3.7 6.9 1.0
HA A:PHE97 3.7 14.6 1.0
CD2 A:PHE97 3.7 12.9 1.0
CA A:ASN98 3.8 12.1 1.0
CA A:PRO99 3.8 10.9 1.0
HZ A:PHE97 3.8 16.6 1.0
HB2 A:ALA162 3.8 8.3 1.0
C4 A:ZD4403 3.9 7.3 1.0
C6 A:ZD4403 3.9 8.7 1.0
C A:PHE97 3.9 12.7 1.0
HB3 A:PRO99 4.0 15.0 1.0
HB1 A:ALA162 4.0 8.3 1.0
HD3 A:PRO99 4.1 17.8 1.0
CA A:PHE97 4.2 12.2 1.0
HE2 A:PHE97 4.2 14.1 1.0
O A:HOH527 4.3 13.8 1.0
HA A:ASN98 4.3 14.5 1.0
HD2 A:PHE97 4.3 15.5 1.0
CD A:PRO99 4.4 14.8 1.0
C5 A:ZD4403 4.4 9.9 1.0
CB A:PHE97 4.4 14.4 1.0
CB A:PRO99 4.4 12.5 1.0
HG21 A:THR288 4.4 11.2 1.0
H A:ALA162 4.5 9.1 1.0
O A:ASP159 4.8 14.6 1.0
HB3 A:ASN98 4.8 16.5 1.0
HB2 A:PHE97 4.9 17.3 1.0
O A:PHE97 4.9 12.7 1.0
CA A:ALA162 4.9 6.9 1.0
CB A:ASN98 4.9 13.7 1.0

Reference:

R.K.Deka, A.Deka, W.Z.Liu, M.V.Norgard, C.A.Brautigam. Inhibition of Bacterial Fmn Transferase: A Potential Avenue For Countering Antimicrobial Resistance. Protein Sci. 2021.
ISSN: ESSN 1469-896X
PubMed: 34796555
DOI: 10.1002/PRO.4241
Page generated: Sun Jul 13 04:06:00 2025

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