Magnesium in PDB 3kr4: Structure of A Protease 3
Enzymatic activity of Structure of A Protease 3
All present enzymatic activity of Structure of A Protease 3:
3.4.11.1;
Protein crystallography data
The structure of Structure of A Protease 3, PDB code: 3kr4
was solved by
S.Mcgowan,
J.C.Whisstock,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
43.15 /
2.00
|
|
Space group
|
P 21 21 21
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
173.561,
178.121,
230.479,
90.00,
90.00,
90.00
|
|
R / Rfree (%)
|
19.2 /
24.2
|
Other elements in 3kr4:
The structure of Structure of A Protease 3 also contains other interesting chemical elements:
Magnesium Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
12;
Binding sites:
The binding sites of Magnesium atom in the Structure of A Protease 3
(pdb code 3kr4). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 12 binding sites of Magnesium where determined in the
Structure of A Protease 3, PDB code: 3kr4:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Magnesium binding site 1 out
of 12 in 3kr4
Go back to
Magnesium Binding Sites List in 3kr4
Magnesium binding site 1 out
of 12 in the Structure of A Protease 3
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Structure of A Protease 3 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg1004
b:24.9
occ:1.00
|
OD1
|
A:ASP459
|
1.8
|
12.2
|
1.0
|
|
OD2
|
A:ASP379
|
2.0
|
7.4
|
1.0
|
|
OE1
|
A:GLU461
|
2.2
|
9.4
|
1.0
|
|
O2
|
A:BES1003
|
2.3
|
20.1
|
1.0
|
|
O
|
A:ASP459
|
2.5
|
11.2
|
1.0
|
|
CG
|
A:ASP379
|
2.8
|
8.2
|
1.0
|
|
OD1
|
A:ASP379
|
2.9
|
9.1
|
1.0
|
|
CG
|
A:ASP459
|
2.9
|
12.6
|
1.0
|
|
O3
|
A:BES1003
|
3.0
|
29.2
|
1.0
|
|
CD
|
A:GLU461
|
3.2
|
11.1
|
1.0
|
|
C
|
A:ASP459
|
3.2
|
10.2
|
1.0
|
|
ZN
|
A:ZN1001
|
3.3
|
39.4
|
1.0
|
|
C2
|
A:BES1003
|
3.3
|
27.2
|
1.0
|
|
C3
|
A:BES1003
|
3.4
|
30.6
|
1.0
|
|
CA
|
A:ASP459
|
3.4
|
10.5
|
1.0
|
|
OE2
|
A:GLU461
|
3.5
|
10.4
|
1.0
|
|
NZ
|
A:LYS386
|
3.6
|
11.2
|
1.0
|
|
CB
|
A:ASP459
|
3.7
|
10.5
|
1.0
|
|
CE
|
A:LYS386
|
3.8
|
9.6
|
1.0
|
|
OD2
|
A:ASP459
|
3.8
|
16.4
|
1.0
|
|
C1
|
A:BES1003
|
3.9
|
26.0
|
1.0
|
|
CB
|
A:ASP379
|
4.2
|
7.0
|
1.0
|
|
ND2
|
A:ASN432
|
4.3
|
7.9
|
1.0
|
|
N1
|
A:BES1003
|
4.4
|
33.2
|
1.0
|
|
N2
|
A:BES1003
|
4.4
|
20.1
|
1.0
|
|
CA
|
A:GLY381
|
4.5
|
7.9
|
1.0
|
|
N
|
A:ALA460
|
4.5
|
9.9
|
1.0
|
|
O2
|
A:CO31002
|
4.5
|
14.2
|
1.0
|
|
N
|
A:GLU461
|
4.6
|
8.6
|
1.0
|
|
CG
|
A:GLU461
|
4.6
|
9.2
|
1.0
|
|
N
|
A:GLY381
|
4.7
|
7.8
|
1.0
|
|
N
|
A:ASP459
|
4.8
|
9.2
|
1.0
|
|
OD2
|
A:ASP399
|
4.9
|
12.5
|
1.0
|
|
O
|
A:THR458
|
5.0
|
9.2
|
1.0
|
|
CA
|
A:ALA460
|
5.0
|
10.0
|
1.0
|
|
Magnesium binding site 2 out
of 12 in 3kr4
Go back to
Magnesium Binding Sites List in 3kr4
Magnesium binding site 2 out
of 12 in the Structure of A Protease 3
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Structure of A Protease 3 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg1004
b:16.5
occ:1.00
|
OD1
|
B:ASP459
|
2.0
|
11.1
|
1.0
|
|
OD2
|
B:ASP379
|
2.1
|
8.5
|
1.0
|
|
O2
|
B:BES1003
|
2.1
|
19.9
|
1.0
|
|
OE1
|
B:GLU461
|
2.2
|
12.4
|
1.0
|
|
O
|
B:ASP459
|
2.3
|
10.6
|
1.0
|
|
CG
|
B:ASP379
|
2.9
|
9.6
|
1.0
|
|
CG
|
B:ASP459
|
3.0
|
11.1
|
1.0
|
|
C2
|
B:BES1003
|
3.1
|
25.7
|
1.0
|
|
OD1
|
B:ASP379
|
3.1
|
7.7
|
1.0
|
|
C
|
B:ASP459
|
3.1
|
10.0
|
1.0
|
|
O3
|
B:BES1003
|
3.1
|
30.4
|
1.0
|
|
CD
|
B:GLU461
|
3.1
|
11.2
|
1.0
|
|
ZN
|
B:ZN1001
|
3.2
|
37.6
|
1.0
|
|
C3
|
B:BES1003
|
3.2
|
29.2
|
1.0
|
|
CA
|
B:ASP459
|
3.4
|
8.6
|
1.0
|
|
OE2
|
B:GLU461
|
3.4
|
11.8
|
1.0
|
|
C1
|
B:BES1003
|
3.8
|
24.0
|
1.0
|
|
CB
|
B:ASP459
|
3.8
|
8.5
|
1.0
|
|
NZ
|
B:LYS386
|
3.9
|
10.3
|
1.0
|
|
OD2
|
B:ASP459
|
4.0
|
12.8
|
1.0
|
|
CE
|
B:LYS386
|
4.0
|
7.6
|
1.0
|
|
N2
|
B:BES1003
|
4.2
|
17.6
|
1.0
|
|
N1
|
B:BES1003
|
4.2
|
31.6
|
1.0
|
|
O2
|
B:CO31002
|
4.2
|
11.8
|
1.0
|
|
N
|
B:ALA460
|
4.3
|
9.3
|
1.0
|
|
N
|
B:GLU461
|
4.3
|
10.1
|
1.0
|
|
CB
|
B:ASP379
|
4.4
|
9.0
|
1.0
|
|
ND2
|
B:ASN432
|
4.5
|
8.8
|
1.0
|
|
CG
|
B:GLU461
|
4.5
|
8.4
|
1.0
|
|
CA
|
B:GLY381
|
4.7
|
7.6
|
1.0
|
|
CA
|
B:ALA460
|
4.7
|
10.0
|
1.0
|
|
N
|
B:ASP459
|
4.8
|
7.0
|
1.0
|
|
OD2
|
B:ASP399
|
4.9
|
12.1
|
1.0
|
|
CB
|
B:GLU461
|
5.0
|
9.8
|
1.0
|
|
NZ
|
B:LYS374
|
5.0
|
8.2
|
1.0
|
|
C4
|
B:BES1003
|
5.0
|
35.8
|
1.0
|
|
Magnesium binding site 3 out
of 12 in 3kr4
Go back to
Magnesium Binding Sites List in 3kr4
Magnesium binding site 3 out
of 12 in the Structure of A Protease 3
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Structure of A Protease 3 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg1004
b:27.1
occ:1.00
|
OD1
|
C:ASP459
|
1.9
|
11.8
|
1.0
|
|
OD2
|
C:ASP379
|
2.1
|
9.0
|
1.0
|
|
O
|
C:ASP459
|
2.2
|
10.3
|
1.0
|
|
O2
|
C:BES1003
|
2.2
|
22.4
|
1.0
|
|
OE1
|
C:GLU461
|
2.4
|
8.1
|
1.0
|
|
O3
|
C:BES1003
|
2.6
|
28.2
|
1.0
|
|
CG
|
C:ASP459
|
2.9
|
12.1
|
1.0
|
|
C3
|
C:BES1003
|
3.0
|
27.6
|
1.0
|
|
CG
|
C:ASP379
|
3.1
|
10.6
|
1.0
|
|
C2
|
C:BES1003
|
3.1
|
26.8
|
1.0
|
|
C
|
C:ASP459
|
3.1
|
11.0
|
1.0
|
|
OD1
|
C:ASP379
|
3.3
|
10.4
|
1.0
|
|
ZN
|
C:ZN1001
|
3.3
|
39.1
|
1.0
|
|
CD
|
C:GLU461
|
3.5
|
10.2
|
1.0
|
|
NZ
|
C:LYS386
|
3.5
|
11.6
|
1.0
|
|
CA
|
C:ASP459
|
3.5
|
10.6
|
1.0
|
|
OD2
|
C:ASP459
|
3.6
|
12.2
|
1.0
|
|
C1
|
C:BES1003
|
3.7
|
24.4
|
1.0
|
|
CB
|
C:ASP459
|
3.7
|
10.9
|
1.0
|
|
OE2
|
C:GLU461
|
3.8
|
11.6
|
1.0
|
|
CE
|
C:LYS386
|
3.9
|
11.9
|
1.0
|
|
N2
|
C:BES1003
|
4.0
|
24.3
|
1.0
|
|
N1
|
C:BES1003
|
4.1
|
30.0
|
1.0
|
|
O1
|
C:CO31002
|
4.3
|
12.9
|
1.0
|
|
N
|
C:ALA460
|
4.4
|
9.7
|
1.0
|
|
CB
|
C:ASP379
|
4.5
|
8.6
|
1.0
|
|
N
|
C:GLU461
|
4.5
|
9.5
|
1.0
|
|
C4
|
C:BES1003
|
4.7
|
33.9
|
1.0
|
|
ND2
|
C:ASN432
|
4.8
|
9.4
|
1.0
|
|
CA
|
C:GLY381
|
4.8
|
8.4
|
1.0
|
|
CA
|
C:ALA460
|
4.8
|
9.8
|
1.0
|
|
CG
|
C:GLU461
|
4.9
|
8.5
|
1.0
|
|
N
|
C:ASP459
|
4.9
|
10.1
|
1.0
|
|
Magnesium binding site 4 out
of 12 in 3kr4
Go back to
Magnesium Binding Sites List in 3kr4
Magnesium binding site 4 out
of 12 in the Structure of A Protease 3
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Structure of A Protease 3 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg1004
b:28.2
occ:1.00
|
O2
|
D:BES1003
|
2.0
|
13.3
|
1.0
|
|
OD2
|
D:ASP379
|
2.0
|
9.2
|
1.0
|
|
OD1
|
D:ASP459
|
2.0
|
12.0
|
1.0
|
|
OE1
|
D:GLU461
|
2.2
|
12.2
|
1.0
|
|
O
|
D:ASP459
|
2.2
|
9.3
|
1.0
|
|
CG
|
D:ASP379
|
2.9
|
10.2
|
1.0
|
|
CG
|
D:ASP459
|
3.1
|
11.6
|
1.0
|
|
O3
|
D:BES1003
|
3.1
|
22.8
|
1.0
|
|
OD1
|
D:ASP379
|
3.1
|
9.0
|
1.0
|
|
C2
|
D:BES1003
|
3.1
|
22.8
|
1.0
|
|
ZN
|
D:ZN1001
|
3.1
|
34.2
|
1.0
|
|
CD
|
D:GLU461
|
3.1
|
13.5
|
1.0
|
|
C
|
D:ASP459
|
3.1
|
9.3
|
1.0
|
|
C3
|
D:BES1003
|
3.3
|
23.2
|
1.0
|
|
OE2
|
D:GLU461
|
3.3
|
13.5
|
1.0
|
|
CA
|
D:ASP459
|
3.5
|
9.6
|
1.0
|
|
NZ
|
D:LYS386
|
3.8
|
12.8
|
1.0
|
|
C1
|
D:BES1003
|
3.8
|
23.3
|
1.0
|
|
CB
|
D:ASP459
|
3.8
|
9.7
|
1.0
|
|
OD2
|
D:ASP459
|
3.9
|
12.7
|
1.0
|
|
N2
|
D:BES1003
|
4.0
|
20.8
|
1.0
|
|
CE
|
D:LYS386
|
4.0
|
11.9
|
1.0
|
|
O1
|
D:CO31002
|
4.1
|
11.6
|
1.0
|
|
N1
|
D:BES1003
|
4.3
|
24.7
|
1.0
|
|
CB
|
D:ASP379
|
4.3
|
8.5
|
1.0
|
|
N
|
D:ALA460
|
4.4
|
8.6
|
1.0
|
|
N
|
D:GLU461
|
4.5
|
10.0
|
1.0
|
|
ND2
|
D:ASN432
|
4.5
|
8.4
|
1.0
|
|
CG
|
D:GLU461
|
4.5
|
11.1
|
1.0
|
|
CA
|
D:GLY381
|
4.8
|
7.5
|
1.0
|
|
OD2
|
D:ASP399
|
4.8
|
9.9
|
1.0
|
|
N
|
D:ASP459
|
4.9
|
9.2
|
1.0
|
|
CA
|
D:ALA460
|
4.9
|
8.2
|
1.0
|
|
NZ
|
D:LYS374
|
4.9
|
4.4
|
1.0
|
|
O
|
D:THR458
|
5.0
|
10.3
|
1.0
|
|
Magnesium binding site 5 out
of 12 in 3kr4
Go back to
Magnesium Binding Sites List in 3kr4
Magnesium binding site 5 out
of 12 in the Structure of A Protease 3
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 5 of Structure of A Protease 3 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mg1004
b:26.4
occ:1.00
|
OE1
|
E:GLU461
|
1.8
|
10.7
|
1.0
|
|
O
|
E:ASP459
|
2.1
|
11.6
|
1.0
|
|
OD1
|
E:ASP459
|
2.1
|
12.2
|
1.0
|
|
OD2
|
E:ASP379
|
2.2
|
10.2
|
1.0
|
|
O2
|
E:BES1003
|
2.3
|
19.8
|
1.0
|
|
CD
|
E:GLU461
|
2.8
|
12.2
|
1.0
|
|
C
|
E:ASP459
|
2.9
|
11.9
|
1.0
|
|
CG
|
E:ASP379
|
3.0
|
10.5
|
1.0
|
|
ZN
|
E:ZN1001
|
3.1
|
38.3
|
1.0
|
|
OD1
|
E:ASP379
|
3.1
|
11.7
|
1.0
|
|
OE2
|
E:GLU461
|
3.2
|
11.9
|
1.0
|
|
CG
|
E:ASP459
|
3.2
|
12.6
|
1.0
|
|
O3
|
E:BES1003
|
3.2
|
29.2
|
1.0
|
|
CA
|
E:ASP459
|
3.3
|
11.6
|
1.0
|
|
C2
|
E:BES1003
|
3.5
|
24.6
|
1.0
|
|
C3
|
E:BES1003
|
3.5
|
27.7
|
1.0
|
|
CB
|
E:ASP459
|
3.8
|
11.6
|
1.0
|
|
N
|
E:GLU461
|
4.0
|
10.3
|
1.0
|
|
N
|
E:ALA460
|
4.0
|
11.1
|
1.0
|
|
NZ
|
E:LYS386
|
4.0
|
14.6
|
1.0
|
|
O3
|
E:CO31002
|
4.2
|
17.8
|
1.0
|
|
OD2
|
E:ASP459
|
4.2
|
10.7
|
1.0
|
|
CG
|
E:GLU461
|
4.2
|
10.0
|
1.0
|
|
ND2
|
E:ASN432
|
4.2
|
9.4
|
1.0
|
|
C1
|
E:BES1003
|
4.3
|
24.9
|
1.0
|
|
N1
|
E:BES1003
|
4.4
|
29.4
|
1.0
|
|
CB
|
E:ASP379
|
4.4
|
9.9
|
1.0
|
|
CA
|
E:ALA460
|
4.5
|
11.1
|
1.0
|
|
N2
|
E:BES1003
|
4.5
|
19.6
|
1.0
|
|
CE
|
E:LYS386
|
4.5
|
11.6
|
1.0
|
|
N
|
E:ASP459
|
4.6
|
11.3
|
1.0
|
|
CB
|
E:GLU461
|
4.6
|
10.4
|
1.0
|
|
O
|
E:THR458
|
4.6
|
11.1
|
1.0
|
|
CA
|
E:GLY381
|
4.7
|
10.7
|
1.0
|
|
C
|
E:ALA460
|
4.8
|
11.1
|
1.0
|
|
CA
|
E:GLU461
|
4.9
|
10.4
|
1.0
|
|
OD2
|
E:ASP399
|
4.9
|
9.7
|
1.0
|
|
NZ
|
E:LYS374
|
5.0
|
10.3
|
1.0
|
|
Magnesium binding site 6 out
of 12 in 3kr4
Go back to
Magnesium Binding Sites List in 3kr4
Magnesium binding site 6 out
of 12 in the Structure of A Protease 3
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 6 of Structure of A Protease 3 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Mg1004
b:37.5
occ:1.00
|
OD1
|
F:ASP459
|
1.9
|
11.5
|
1.0
|
|
OD2
|
F:ASP379
|
2.0
|
13.3
|
1.0
|
|
O2
|
F:BES1003
|
2.3
|
13.3
|
1.0
|
|
OE1
|
F:GLU461
|
2.3
|
12.1
|
1.0
|
|
O
|
F:ASP459
|
2.3
|
11.1
|
1.0
|
|
CG
|
F:ASP379
|
2.8
|
12.8
|
1.0
|
|
O3
|
F:BES1003
|
3.0
|
27.7
|
1.0
|
|
CG
|
F:ASP459
|
3.0
|
13.1
|
1.0
|
|
OD1
|
F:ASP379
|
3.0
|
14.6
|
1.0
|
|
ZN
|
F:ZN1001
|
3.1
|
40.9
|
1.0
|
|
C2
|
F:BES1003
|
3.2
|
22.7
|
1.0
|
|
C3
|
F:BES1003
|
3.2
|
28.1
|
1.0
|
|
C
|
F:ASP459
|
3.2
|
10.8
|
1.0
|
|
CD
|
F:GLU461
|
3.2
|
11.1
|
1.0
|
|
OE2
|
F:GLU461
|
3.4
|
9.6
|
1.0
|
|
CA
|
F:ASP459
|
3.5
|
10.0
|
1.0
|
|
NZ
|
F:LYS386
|
3.7
|
15.4
|
1.0
|
|
C1
|
F:BES1003
|
3.8
|
22.4
|
1.0
|
|
CB
|
F:ASP459
|
3.8
|
10.7
|
1.0
|
|
OD2
|
F:ASP459
|
3.9
|
13.3
|
1.0
|
|
CE
|
F:LYS386
|
4.0
|
11.6
|
1.0
|
|
N2
|
F:BES1003
|
4.0
|
19.6
|
1.0
|
|
N1
|
F:BES1003
|
4.1
|
32.0
|
1.0
|
|
CB
|
F:ASP379
|
4.3
|
11.1
|
1.0
|
|
O1
|
F:CO31002
|
4.3
|
12.6
|
1.0
|
|
N
|
F:ALA460
|
4.4
|
10.2
|
1.0
|
|
N
|
F:GLU461
|
4.5
|
8.0
|
1.0
|
|
ND2
|
F:ASN432
|
4.6
|
9.3
|
1.0
|
|
CG
|
F:GLU461
|
4.6
|
10.6
|
1.0
|
|
CA
|
F:GLY381
|
4.7
|
11.1
|
1.0
|
|
OD2
|
F:ASP399
|
4.8
|
20.6
|
1.0
|
|
C4
|
F:BES1003
|
4.9
|
35.2
|
1.0
|
|
NZ
|
F:LYS374
|
4.9
|
5.2
|
1.0
|
|
N
|
F:ASP459
|
4.9
|
7.8
|
1.0
|
|
N
|
F:GLY381
|
4.9
|
11.1
|
1.0
|
|
CA
|
F:ALA460
|
5.0
|
10.1
|
1.0
|
|
Magnesium binding site 7 out
of 12 in 3kr4
Go back to
Magnesium Binding Sites List in 3kr4
Magnesium binding site 7 out
of 12 in the Structure of A Protease 3
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 7 of Structure of A Protease 3 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Mg1004
b:23.7
occ:1.00
|
OD2
|
G:ASP379
|
2.0
|
7.0
|
1.0
|
|
OD1
|
G:ASP459
|
2.0
|
11.9
|
1.0
|
|
O2
|
G:BES1003
|
2.2
|
13.8
|
1.0
|
|
OE1
|
G:GLU461
|
2.2
|
8.5
|
1.0
|
|
O
|
G:ASP459
|
2.4
|
11.3
|
1.0
|
|
CG
|
G:ASP379
|
2.8
|
8.2
|
1.0
|
|
OD1
|
G:ASP379
|
3.0
|
7.9
|
1.0
|
|
O3
|
G:BES1003
|
3.0
|
28.3
|
1.0
|
|
CG
|
G:ASP459
|
3.0
|
12.5
|
1.0
|
|
ZN
|
G:ZN1001
|
3.1
|
38.2
|
1.0
|
|
CD
|
G:GLU461
|
3.2
|
11.0
|
1.0
|
|
C2
|
G:BES1003
|
3.2
|
24.0
|
1.0
|
|
C
|
G:ASP459
|
3.2
|
10.3
|
1.0
|
|
C3
|
G:BES1003
|
3.3
|
26.3
|
1.0
|
|
OE2
|
G:GLU461
|
3.5
|
11.1
|
1.0
|
|
CA
|
G:ASP459
|
3.5
|
10.2
|
1.0
|
|
NZ
|
G:LYS386
|
3.6
|
11.6
|
1.0
|
|
C1
|
G:BES1003
|
3.8
|
22.9
|
1.0
|
|
CB
|
G:ASP459
|
3.8
|
10.7
|
1.0
|
|
OD2
|
G:ASP459
|
3.9
|
16.2
|
1.0
|
|
CE
|
G:LYS386
|
3.9
|
8.9
|
1.0
|
|
N2
|
G:BES1003
|
4.1
|
15.9
|
1.0
|
|
N1
|
G:BES1003
|
4.2
|
30.1
|
1.0
|
|
CB
|
G:ASP379
|
4.2
|
7.4
|
1.0
|
|
O2
|
G:CO31002
|
4.4
|
11.8
|
1.0
|
|
N
|
G:ALA460
|
4.4
|
9.1
|
1.0
|
|
ND2
|
G:ASN432
|
4.4
|
7.5
|
1.0
|
|
N
|
G:GLU461
|
4.5
|
8.5
|
1.0
|
|
CG
|
G:GLU461
|
4.6
|
9.8
|
1.0
|
|
CA
|
G:GLY381
|
4.7
|
7.9
|
1.0
|
|
OD2
|
G:ASP399
|
4.8
|
12.9
|
1.0
|
|
N
|
G:ASP459
|
4.9
|
9.1
|
1.0
|
|
CA
|
G:ALA460
|
4.9
|
9.8
|
1.0
|
|
N
|
G:GLY381
|
4.9
|
7.2
|
1.0
|
|
C4
|
G:BES1003
|
5.0
|
32.6
|
1.0
|
|
Magnesium binding site 8 out
of 12 in 3kr4
Go back to
Magnesium Binding Sites List in 3kr4
Magnesium binding site 8 out
of 12 in the Structure of A Protease 3
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 8 of Structure of A Protease 3 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Mg1004
b:40.7
occ:1.00
|
OD1
|
H:ASP459
|
1.8
|
11.7
|
1.0
|
|
OD2
|
H:ASP379
|
2.2
|
8.3
|
1.0
|
|
O
|
H:ASP459
|
2.2
|
10.4
|
1.0
|
|
OE1
|
H:GLU461
|
2.3
|
11.3
|
1.0
|
|
O2
|
H:BES1003
|
2.3
|
16.5
|
1.0
|
|
CG
|
H:ASP459
|
2.9
|
11.4
|
1.0
|
|
O3
|
H:BES1003
|
3.0
|
22.7
|
1.0
|
|
CG
|
H:ASP379
|
3.0
|
9.3
|
1.0
|
|
C
|
H:ASP459
|
3.1
|
9.8
|
1.0
|
|
C3
|
H:BES1003
|
3.2
|
24.5
|
1.0
|
|
ZN
|
H:ZN1001
|
3.2
|
34.8
|
1.0
|
|
CD
|
H:GLU461
|
3.3
|
10.8
|
1.0
|
|
C2
|
H:BES1003
|
3.3
|
19.6
|
1.0
|
|
OD1
|
H:ASP379
|
3.3
|
6.6
|
1.0
|
|
CA
|
H:ASP459
|
3.3
|
8.6
|
1.0
|
|
OE2
|
H:GLU461
|
3.5
|
10.3
|
1.0
|
|
CB
|
H:ASP459
|
3.7
|
8.2
|
1.0
|
|
NZ
|
H:LYS386
|
3.7
|
9.6
|
1.0
|
|
OD2
|
H:ASP459
|
3.8
|
13.5
|
1.0
|
|
C1
|
H:BES1003
|
3.8
|
19.2
|
1.0
|
|
CE
|
H:LYS386
|
4.0
|
7.8
|
1.0
|
|
N1
|
H:BES1003
|
4.1
|
25.2
|
1.0
|
|
N2
|
H:BES1003
|
4.1
|
15.8
|
1.0
|
|
O2
|
H:CO31002
|
4.2
|
10.3
|
1.0
|
|
N
|
H:ALA460
|
4.3
|
9.1
|
1.0
|
|
N
|
H:GLU461
|
4.3
|
10.4
|
1.0
|
|
CB
|
H:ASP379
|
4.4
|
8.8
|
1.0
|
|
ND2
|
H:ASN432
|
4.5
|
8.6
|
1.0
|
|
CG
|
H:GLU461
|
4.6
|
8.0
|
1.0
|
|
CA
|
H:GLY381
|
4.7
|
7.3
|
1.0
|
|
CA
|
H:ALA460
|
4.7
|
9.9
|
1.0
|
|
N
|
H:ASP459
|
4.7
|
6.7
|
1.0
|
|
C4
|
H:BES1003
|
4.8
|
30.2
|
1.0
|
|
O
|
H:THR458
|
5.0
|
6.5
|
1.0
|
|
OD2
|
H:ASP399
|
5.0
|
11.4
|
1.0
|
|
Magnesium binding site 9 out
of 12 in 3kr4
Go back to
Magnesium Binding Sites List in 3kr4
Magnesium binding site 9 out
of 12 in the Structure of A Protease 3
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 9 of Structure of A Protease 3 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
I:Mg1004
b:15.1
occ:1.00
|
OE1
|
I:GLU461
|
2.0
|
8.1
|
1.0
|
|
OD1
|
I:ASP459
|
2.0
|
11.6
|
1.0
|
|
OD2
|
I:ASP379
|
2.0
|
8.2
|
1.0
|
|
O2
|
I:BES1003
|
2.2
|
11.2
|
1.0
|
|
O
|
I:ASP459
|
2.2
|
9.6
|
1.0
|
|
CG
|
I:ASP379
|
2.8
|
10.2
|
1.0
|
|
CD
|
I:GLU461
|
2.9
|
9.5
|
1.0
|
|
OD1
|
I:ASP379
|
3.0
|
10.4
|
1.0
|
|
C
|
I:ASP459
|
3.1
|
10.6
|
1.0
|
|
CG
|
I:ASP459
|
3.1
|
11.9
|
1.0
|
|
ZN
|
I:ZN1001
|
3.2
|
36.9
|
1.0
|
|
OE2
|
I:GLU461
|
3.2
|
11.9
|
1.0
|
|
O3
|
I:BES1003
|
3.2
|
25.1
|
1.0
|
|
C2
|
I:BES1003
|
3.4
|
22.5
|
1.0
|
|
CA
|
I:ASP459
|
3.5
|
10.3
|
1.0
|
|
C3
|
I:BES1003
|
3.5
|
24.5
|
1.0
|
|
NZ
|
I:LYS386
|
3.9
|
12.1
|
1.0
|
|
CB
|
I:ASP459
|
3.9
|
10.7
|
1.0
|
|
OD2
|
I:ASP459
|
4.0
|
11.6
|
1.0
|
|
C1
|
I:BES1003
|
4.1
|
22.6
|
1.0
|
|
CE
|
I:LYS386
|
4.2
|
11.4
|
1.0
|
|
N2
|
I:BES1003
|
4.2
|
20.4
|
1.0
|
|
ND2
|
I:ASN432
|
4.3
|
9.7
|
1.0
|
|
N
|
I:GLU461
|
4.3
|
9.1
|
1.0
|
|
O1
|
I:CO31002
|
4.3
|
15.7
|
1.0
|
|
N
|
I:ALA460
|
4.3
|
9.6
|
1.0
|
|
CB
|
I:ASP379
|
4.3
|
8.2
|
1.0
|
|
CG
|
I:GLU461
|
4.4
|
8.4
|
1.0
|
|
N1
|
I:BES1003
|
4.4
|
27.2
|
1.0
|
|
CA
|
I:GLY381
|
4.7
|
8.0
|
1.0
|
|
CA
|
I:ALA460
|
4.8
|
9.4
|
1.0
|
|
CB
|
I:GLU461
|
4.8
|
9.0
|
1.0
|
|
OD2
|
I:ASP399
|
4.8
|
10.4
|
1.0
|
|
N
|
I:ASP459
|
4.9
|
9.7
|
1.0
|
|
O
|
I:THR458
|
4.9
|
8.6
|
1.0
|
|
NZ
|
I:LYS374
|
4.9
|
8.1
|
1.0
|
|
Magnesium binding site 10 out
of 12 in 3kr4
Go back to
Magnesium Binding Sites List in 3kr4
Magnesium binding site 10 out
of 12 in the Structure of A Protease 3
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 10 of Structure of A Protease 3 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
J:Mg1004
b:23.0
occ:1.00
|
OD1
|
J:ASP459
|
1.9
|
11.6
|
1.0
|
|
OD2
|
J:ASP379
|
2.0
|
8.2
|
1.0
|
|
OE2
|
J:GLU461
|
2.2
|
12.9
|
1.0
|
|
O2
|
J:BES1003
|
2.2
|
11.3
|
1.0
|
|
O
|
J:ASP459
|
2.3
|
9.7
|
1.0
|
|
CG
|
J:ASP379
|
2.8
|
10.2
|
1.0
|
|
OD1
|
J:ASP379
|
2.9
|
8.6
|
1.0
|
|
CG
|
J:ASP459
|
2.9
|
11.3
|
1.0
|
|
C
|
J:ASP459
|
3.1
|
9.5
|
1.0
|
|
O3
|
J:BES1003
|
3.1
|
28.9
|
1.0
|
|
CD
|
J:GLU461
|
3.1
|
13.4
|
1.0
|
|
C2
|
J:BES1003
|
3.2
|
23.9
|
1.0
|
|
ZN
|
J:ZN1001
|
3.3
|
38.0
|
1.0
|
|
OE1
|
J:GLU461
|
3.3
|
12.4
|
1.0
|
|
CA
|
J:ASP459
|
3.3
|
9.9
|
1.0
|
|
C3
|
J:BES1003
|
3.3
|
26.1
|
1.0
|
|
CB
|
J:ASP459
|
3.7
|
10.5
|
1.0
|
|
NZ
|
J:LYS386
|
3.7
|
13.5
|
1.0
|
|
OD2
|
J:ASP459
|
3.8
|
12.6
|
1.0
|
|
C1
|
J:BES1003
|
3.8
|
22.4
|
1.0
|
|
CE
|
J:LYS386
|
4.0
|
12.4
|
1.0
|
|
N2
|
J:BES1003
|
4.2
|
23.6
|
1.0
|
|
CB
|
J:ASP379
|
4.3
|
9.1
|
1.0
|
|
N
|
J:ALA460
|
4.3
|
8.3
|
1.0
|
|
O3
|
J:CO31002
|
4.3
|
16.0
|
1.0
|
|
N1
|
J:BES1003
|
4.3
|
30.3
|
1.0
|
|
ND2
|
J:ASN432
|
4.4
|
8.8
|
1.0
|
|
N
|
J:GLU461
|
4.4
|
9.5
|
1.0
|
|
CG
|
J:GLU461
|
4.5
|
11.0
|
1.0
|
|
CA
|
J:GLY381
|
4.5
|
8.8
|
1.0
|
|
N
|
J:ASP459
|
4.7
|
9.7
|
1.0
|
|
CA
|
J:ALA460
|
4.8
|
8.2
|
1.0
|
|
O
|
J:THR458
|
4.9
|
10.1
|
1.0
|
|
N
|
J:GLY381
|
4.9
|
8.9
|
1.0
|
|
OD2
|
J:ASP399
|
4.9
|
9.9
|
1.0
|
|
CB
|
J:GLU461
|
5.0
|
10.4
|
1.0
|
|
Reference:
S.Mcgowan,
C.A.Oellig,
W.A.Birru,
T.T.Caradoc-Davies,
C.M.Stack,
J.Lowther,
T.Skinner-Adams,
A.Mucha,
P.Kafarski,
J.Grembecka,
K.R.Trenholme,
A.M.Buckle,
D.L.Gardiner,
J.P.Dalton,
J.C.Whisstock.
Structure of the Plasmodium Falciparum M17 Aminopeptidase and Significance For the Design of Drugs Targeting the Neutral Exopeptidases Proc.Natl.Acad.Sci.Usa V. 107 2449 2010.
ISSN: ISSN 0027-8424
PubMed: 20133789
DOI: 10.1073/PNAS.0911813107
Page generated: Wed Aug 14 18:12:42 2024
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