Chlorine in PDB 6w9t: Crystal Structure of Neisseria Meningitidis Clpp Protease Complex with Small Molecule Activator ACP1-06
Enzymatic activity of Crystal Structure of Neisseria Meningitidis Clpp Protease Complex with Small Molecule Activator ACP1-06
All present enzymatic activity of Crystal Structure of Neisseria Meningitidis Clpp Protease Complex with Small Molecule Activator ACP1-06:
3.4.21.92;
Protein crystallography data
The structure of Crystal Structure of Neisseria Meningitidis Clpp Protease Complex with Small Molecule Activator ACP1-06, PDB code: 6w9t
was solved by
M.F.Mabanglo,
W.A.Houry,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
97.33 /
1.64
|
Space group
|
P 2 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
97.328,
119.150,
127.763,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
23.7 /
28.2
|
Other elements in 6w9t:
The structure of Crystal Structure of Neisseria Meningitidis Clpp Protease Complex with Small Molecule Activator ACP1-06 also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of Neisseria Meningitidis Clpp Protease Complex with Small Molecule Activator ACP1-06
(pdb code 6w9t). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the
Crystal Structure of Neisseria Meningitidis Clpp Protease Complex with Small Molecule Activator ACP1-06, PDB code: 6w9t:
Jump to Chlorine binding site number:
1;
2;
Chlorine binding site 1 out
of 2 in 6w9t
Go back to
Chlorine Binding Sites List in 6w9t
Chlorine binding site 1 out
of 2 in the Crystal Structure of Neisseria Meningitidis Clpp Protease Complex with Small Molecule Activator ACP1-06
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 1 of Crystal Structure of Neisseria Meningitidis Clpp Protease Complex with Small Molecule Activator ACP1-06 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Cl301
b:58.3
occ:0.56
|
CLB
|
F:KHS301
|
0.0
|
58.3
|
0.6
|
CBB
|
F:KHS301
|
1.8
|
60.5
|
0.6
|
SAV
|
F:KHS301
|
2.1
|
61.2
|
0.4
|
H4
|
F:KHS301
|
2.2
|
71.8
|
0.4
|
H7
|
F:KHS301
|
2.2
|
77.0
|
0.4
|
CAY
|
F:KHS301
|
2.7
|
59.8
|
0.4
|
CBA
|
F:KHS301
|
2.7
|
60.1
|
0.6
|
CAZ
|
F:KHS301
|
2.8
|
57.0
|
0.6
|
CAZ
|
F:KHS301
|
2.8
|
57.0
|
0.4
|
H1
|
F:KHS301
|
2.8
|
72.2
|
0.6
|
CAT
|
F:KHS301
|
2.9
|
64.1
|
0.4
|
CAU
|
F:KHS301
|
3.0
|
61.0
|
0.4
|
H7
|
F:KHS301
|
3.0
|
71.9
|
0.6
|
SAV
|
F:KHS301
|
3.2
|
54.0
|
0.6
|
H9
|
F:KHS301
|
3.2
|
77.3
|
0.6
|
OE2
|
F:GLU31
|
3.3
|
57.0
|
1.0
|
H12
|
F:KHS301
|
3.3
|
82.4
|
0.6
|
NAS
|
F:KHS301
|
3.3
|
66.2
|
0.4
|
H6
|
F:KHS301
|
3.4
|
73.3
|
0.4
|
NAS
|
F:KHS301
|
3.4
|
64.4
|
0.6
|
H9
|
F:KHS301
|
3.5
|
79.5
|
0.4
|
CAT
|
F:KHS301
|
3.5
|
59.9
|
0.6
|
HB3
|
F:GLU31
|
3.6
|
78.9
|
1.0
|
H8
|
F:KHS301
|
3.7
|
77.0
|
0.4
|
H5
|
F:KHS301
|
3.8
|
73.3
|
0.4
|
CAU
|
F:KHS301
|
4.0
|
56.7
|
0.6
|
CAX
|
F:KHS301
|
4.0
|
59.4
|
0.4
|
CAQ
|
F:KHS301
|
4.0
|
69.3
|
0.4
|
CAW
|
F:KHS301
|
4.0
|
59.9
|
0.6
|
CAY
|
F:KHS301
|
4.1
|
56.5
|
0.6
|
H10
|
F:KHS301
|
4.1
|
80.5
|
0.4
|
CBB
|
F:KHS301
|
4.1
|
50.5
|
0.4
|
HD12
|
F:ILE33
|
4.1
|
42.8
|
1.0
|
CAQ
|
F:KHS301
|
4.2
|
69.7
|
0.6
|
OAR
|
F:KHS301
|
4.2
|
70.2
|
0.4
|
CAP
|
F:KHS301
|
4.2
|
68.6
|
0.6
|
H6
|
F:KHS301
|
4.3
|
68.0
|
0.6
|
CD
|
F:GLU31
|
4.4
|
64.2
|
1.0
|
H3
|
F:KHS301
|
4.4
|
71.3
|
0.4
|
HH12
|
F:ARG199
|
4.4
|
73.5
|
1.0
|
H8
|
F:KHS301
|
4.4
|
71.9
|
0.6
|
CB
|
F:GLU31
|
4.5
|
65.7
|
1.0
|
HH22
|
F:ARG199
|
4.6
|
59.5
|
1.0
|
CAX
|
F:KHS301
|
4.6
|
59.9
|
0.6
|
O
|
F:GLU31
|
4.7
|
26.2
|
1.0
|
H11
|
F:KHS301
|
4.7
|
82.4
|
0.6
|
H10
|
F:KHS301
|
4.7
|
82.4
|
0.6
|
H15
|
F:KHS301
|
4.8
|
89.2
|
0.6
|
H2
|
F:KHS301
|
4.8
|
71.8
|
0.6
|
H4
|
F:KHS301
|
4.8
|
67.8
|
0.6
|
H5
|
F:KHS301
|
4.8
|
68.0
|
0.6
|
HE2
|
F:PHE65
|
4.8
|
63.3
|
1.0
|
OAR
|
F:KHS301
|
4.8
|
70.6
|
0.6
|
H15
|
F:KHS301
|
4.8
|
88.7
|
0.4
|
CAO
|
F:KHS301
|
4.9
|
69.5
|
0.6
|
CG
|
F:GLU31
|
4.9
|
81.0
|
1.0
|
HG3
|
F:GLU31
|
4.9
|
97.2
|
1.0
|
CAP
|
F:KHS301
|
4.9
|
67.1
|
0.4
|
HG13
|
F:ILE33
|
4.9
|
29.4
|
1.0
|
CD1
|
F:ILE33
|
4.9
|
35.7
|
1.0
|
HB2
|
F:GLU31
|
5.0
|
78.9
|
1.0
|
HD11
|
F:ILE33
|
5.0
|
42.8
|
1.0
|
|
Chlorine binding site 2 out
of 2 in 6w9t
Go back to
Chlorine Binding Sites List in 6w9t
Chlorine binding site 2 out
of 2 in the Crystal Structure of Neisseria Meningitidis Clpp Protease Complex with Small Molecule Activator ACP1-06
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 2 of Crystal Structure of Neisseria Meningitidis Clpp Protease Complex with Small Molecule Activator ACP1-06 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Cl301
b:24.8
occ:0.44
|
CLB
|
F:KHS301
|
0.0
|
24.8
|
0.4
|
CBB
|
F:KHS301
|
1.8
|
50.5
|
0.4
|
SAV
|
F:KHS301
|
2.1
|
54.0
|
0.6
|
H4
|
F:KHS301
|
2.1
|
67.8
|
0.6
|
H6
|
F:KHS301
|
2.4
|
68.0
|
0.6
|
CAU
|
F:KHS301
|
2.5
|
56.7
|
0.6
|
H5
|
F:KHS301
|
2.5
|
68.0
|
0.6
|
CAY
|
F:KHS301
|
2.7
|
56.5
|
0.6
|
CBA
|
F:KHS301
|
2.8
|
57.8
|
0.4
|
OE1
|
E:GLU56
|
2.8
|
34.3
|
1.0
|
CAZ
|
F:KHS301
|
2.8
|
57.0
|
0.6
|
CAZ
|
F:KHS301
|
2.8
|
57.0
|
0.4
|
H1
|
F:KHS301
|
2.8
|
69.4
|
0.4
|
H6
|
F:KHS301
|
2.9
|
73.3
|
0.4
|
HB3
|
E:GLU56
|
2.9
|
32.7
|
1.0
|
O
|
E:LEU53
|
3.0
|
31.9
|
1.0
|
HD23
|
E:LEU53
|
3.2
|
31.0
|
1.0
|
H5
|
F:KHS301
|
3.3
|
73.3
|
0.4
|
HB3
|
E:SER57
|
3.3
|
56.0
|
1.0
|
CAU
|
F:KHS301
|
3.3
|
61.0
|
0.4
|
SAV
|
F:KHS301
|
3.3
|
61.2
|
0.4
|
HA
|
E:LEU53
|
3.3
|
29.3
|
1.0
|
HH22
|
F:ARG199
|
3.3
|
59.5
|
1.0
|
H
|
E:SER57
|
3.4
|
31.2
|
1.0
|
HB3
|
E:LEU53
|
3.4
|
21.9
|
1.0
|
HH21
|
F:ARG199
|
3.5
|
59.5
|
1.0
|
CD
|
E:GLU56
|
3.6
|
23.5
|
1.0
|
HG2
|
E:GLU56
|
3.7
|
43.3
|
1.0
|
N
|
E:SER57
|
3.7
|
26.0
|
1.0
|
NH2
|
F:ARG199
|
3.7
|
49.5
|
1.0
|
CB
|
E:GLU56
|
3.8
|
27.2
|
1.0
|
C
|
E:LEU53
|
3.8
|
35.7
|
1.0
|
CA
|
E:LEU53
|
3.9
|
24.4
|
1.0
|
CG
|
E:GLU56
|
3.9
|
36.1
|
1.0
|
CAT
|
F:KHS301
|
4.0
|
59.9
|
0.6
|
CB
|
E:SER57
|
4.0
|
46.7
|
1.0
|
HA
|
E:SER57
|
4.0
|
25.9
|
1.0
|
CAX
|
F:KHS301
|
4.0
|
59.9
|
0.6
|
CAW
|
F:KHS301
|
4.1
|
60.3
|
0.4
|
CB
|
E:LEU53
|
4.1
|
18.2
|
1.0
|
CAY
|
F:KHS301
|
4.1
|
59.8
|
0.4
|
CD2
|
E:LEU53
|
4.1
|
25.8
|
1.0
|
HB2
|
E:SER57
|
4.1
|
56.0
|
1.0
|
CBB
|
F:KHS301
|
4.1
|
60.5
|
0.6
|
CA
|
E:SER57
|
4.1
|
21.6
|
1.0
|
C
|
E:GLU56
|
4.2
|
41.5
|
1.0
|
H7
|
F:KHS301
|
4.3
|
71.9
|
0.6
|
HD21
|
E:LEU53
|
4.4
|
31.0
|
1.0
|
H3
|
F:KHS301
|
4.4
|
71.8
|
0.6
|
O
|
F:HOH402
|
4.4
|
66.8
|
1.0
|
H9
|
F:KHS301
|
4.4
|
77.3
|
0.6
|
HB2
|
E:GLU56
|
4.5
|
32.7
|
1.0
|
H8
|
F:KHS301
|
4.5
|
71.9
|
0.6
|
CA
|
E:GLU56
|
4.5
|
35.9
|
1.0
|
CAX
|
F:KHS301
|
4.6
|
59.4
|
0.4
|
OE2
|
E:GLU56
|
4.6
|
27.9
|
1.0
|
H
|
E:GLU56
|
4.7
|
31.3
|
1.0
|
HD22
|
E:LEU53
|
4.7
|
31.0
|
1.0
|
NAS
|
F:KHS301
|
4.7
|
64.4
|
0.6
|
CG
|
E:LEU53
|
4.8
|
19.8
|
1.0
|
H2
|
F:KHS301
|
4.8
|
72.4
|
0.4
|
CAT
|
F:KHS301
|
4.8
|
64.1
|
0.4
|
H4
|
F:KHS301
|
4.8
|
71.8
|
0.4
|
HG3
|
E:GLU56
|
4.8
|
43.3
|
1.0
|
CZ
|
F:ARG199
|
4.9
|
52.0
|
1.0
|
H9
|
F:KHS301
|
4.9
|
79.5
|
0.4
|
HB2
|
E:LEU53
|
4.9
|
21.9
|
1.0
|
N
|
E:GLU56
|
5.0
|
26.1
|
1.0
|
HG22
|
E:ILE88
|
5.0
|
43.6
|
1.0
|
O
|
E:GLU56
|
5.0
|
28.7
|
1.0
|
|
Reference:
G.Binepal,
M.F.Mabanglo,
J.D.Goodreid,
E.Leung,
M.M.Barghash,
K.S.Wong,
F.Lin,
M.Cossette,
J.Bansagi,
B.Song,
V.H.Balasco Serrao,
E.F.Pai,
R.A.Batey,
S.D.Gray-Owen,
W.A.Houry.
Development of Antibiotics That Dysregulate the Neisserial Clpp Protease. Acs Infect Dis. 2020.
ISSN: ESSN 2373-8227
PubMed: 33237740
DOI: 10.1021/ACSINFECDIS.0C00599
Page generated: Mon Jul 29 16:41:15 2024
|