Zinc in PDB 3t9u: Cnqx Bound to An Oxidized Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2
Protein crystallography data
The structure of Cnqx Bound to An Oxidized Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2, PDB code: 3t9u
was solved by
A.H.Ahmed,
R.E.Oswald,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
33.50 /
1.97
|
Space group
|
P 21 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
114.724,
165.243,
47.651,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
16.5 /
21.9
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Cnqx Bound to An Oxidized Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2
(pdb code 3t9u). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 5 binding sites of Zinc where determined in the
Cnqx Bound to An Oxidized Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2, PDB code: 3t9u:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
Zinc binding site 1 out
of 5 in 3t9u
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Zinc Binding Sites List in 3t9u
Zinc binding site 1 out
of 5 in the Cnqx Bound to An Oxidized Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Cnqx Bound to An Oxidized Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1
b:27.7
occ:1.00
|
NE2
|
A:HIS23
|
2.2
|
21.8
|
1.0
|
CE1
|
A:HIS23
|
3.1
|
26.9
|
1.0
|
CD2
|
A:HIS23
|
3.3
|
19.2
|
1.0
|
ND1
|
A:HIS23
|
4.3
|
21.1
|
1.0
|
CG
|
A:HIS23
|
4.4
|
19.1
|
1.0
|
CB
|
A:MET19
|
5.0
|
19.0
|
1.0
|
|
Zinc binding site 2 out
of 5 in 3t9u
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Zinc Binding Sites List in 3t9u
Zinc binding site 2 out
of 5 in the Cnqx Bound to An Oxidized Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Cnqx Bound to An Oxidized Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn3
b:21.9
occ:1.00
|
OE1
|
B:GLU24
|
2.4
|
30.3
|
1.0
|
CD
|
B:GLU24
|
2.4
|
29.9
|
1.0
|
OE2
|
B:GLU24
|
2.5
|
29.3
|
1.0
|
NE2
|
B:HIS23
|
2.5
|
23.9
|
1.0
|
CD2
|
B:HIS23
|
3.3
|
23.3
|
1.0
|
CG
|
B:GLU24
|
3.4
|
30.3
|
1.0
|
CE1
|
B:HIS23
|
3.6
|
24.1
|
1.0
|
CG
|
B:HIS23
|
4.5
|
24.3
|
1.0
|
ND1
|
B:HIS23
|
4.6
|
19.9
|
1.0
|
CB
|
B:GLU24
|
4.8
|
30.6
|
1.0
|
|
Zinc binding site 3 out
of 5 in 3t9u
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Zinc Binding Sites List in 3t9u
Zinc binding site 3 out
of 5 in the Cnqx Bound to An Oxidized Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Cnqx Bound to An Oxidized Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn262
b:71.4
occ:1.00
|
OE1
|
B:GLU42
|
2.3
|
37.0
|
1.0
|
NE2
|
B:HIS46
|
2.5
|
46.7
|
1.0
|
CD2
|
B:HIS46
|
3.4
|
43.2
|
1.0
|
CD
|
B:GLU42
|
3.5
|
35.0
|
1.0
|
CE1
|
B:HIS46
|
3.5
|
48.1
|
1.0
|
OE2
|
B:GLU42
|
4.0
|
42.5
|
1.0
|
CD2
|
B:LEU241
|
4.1
|
25.0
|
1.0
|
OE1
|
B:GLN244
|
4.3
|
44.9
|
1.0
|
NZ
|
B:LYS45
|
4.5
|
51.9
|
1.0
|
CD
|
B:LYS45
|
4.6
|
45.0
|
1.0
|
CG
|
B:HIS46
|
4.6
|
42.3
|
1.0
|
ND1
|
B:HIS46
|
4.6
|
44.6
|
1.0
|
CG
|
B:GLU42
|
4.6
|
27.6
|
1.0
|
CB
|
B:GLU42
|
4.8
|
23.7
|
1.0
|
CE
|
B:LYS45
|
5.0
|
48.6
|
1.0
|
|
Zinc binding site 4 out
of 5 in 3t9u
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Zinc Binding Sites List in 3t9u
Zinc binding site 4 out
of 5 in the Cnqx Bound to An Oxidized Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Cnqx Bound to An Oxidized Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn2
b:18.1
occ:1.00
|
OE1
|
C:GLU166
|
1.7
|
15.2
|
1.0
|
OE1
|
A:GLU42
|
2.0
|
17.8
|
1.0
|
NE2
|
A:HIS46
|
2.1
|
21.4
|
1.0
|
CD
|
C:GLU166
|
2.5
|
22.4
|
1.0
|
OE2
|
C:GLU166
|
2.7
|
19.3
|
1.0
|
CD
|
A:GLU42
|
2.9
|
19.2
|
1.0
|
CD2
|
A:HIS46
|
3.0
|
19.0
|
1.0
|
CE1
|
A:HIS46
|
3.1
|
25.1
|
1.0
|
OE2
|
A:GLU42
|
3.2
|
17.0
|
1.0
|
CG
|
C:GLU166
|
4.0
|
17.0
|
1.0
|
CG
|
A:HIS46
|
4.1
|
21.2
|
1.0
|
ND1
|
A:HIS46
|
4.2
|
20.2
|
1.0
|
CD2
|
A:LEU241
|
4.2
|
20.1
|
1.0
|
CG
|
A:GLU42
|
4.3
|
14.1
|
1.0
|
N
|
C:SER168
|
4.4
|
14.3
|
1.0
|
CB
|
A:GLU42
|
4.6
|
11.7
|
1.0
|
CB
|
C:GLU166
|
4.7
|
18.3
|
1.0
|
O
|
C:ALA165
|
4.8
|
15.9
|
1.0
|
CB
|
C:SER168
|
4.8
|
12.1
|
1.0
|
CD
|
A:LYS45
|
4.8
|
35.2
|
1.0
|
CE
|
A:LYS45
|
4.9
|
36.9
|
1.0
|
CA
|
C:SER168
|
4.9
|
13.0
|
1.0
|
CA
|
C:PRO167
|
5.0
|
17.3
|
1.0
|
CA
|
C:GLU166
|
5.0
|
17.0
|
1.0
|
|
Zinc binding site 5 out
of 5 in 3t9u
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Zinc Binding Sites List in 3t9u
Zinc binding site 5 out
of 5 in the Cnqx Bound to An Oxidized Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 5 of Cnqx Bound to An Oxidized Double Cysteine Mutant (A452C/S652C) of the Ligand Binding Domain of GLUA2 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn262
b:18.3
occ:1.00
|
NE2
|
C:HIS46
|
1.9
|
10.8
|
1.0
|
OE1
|
C:GLU42
|
2.0
|
18.9
|
1.0
|
CD2
|
C:HIS46
|
2.8
|
16.6
|
1.0
|
CE1
|
C:HIS46
|
2.9
|
21.1
|
1.0
|
CD
|
C:GLU42
|
2.9
|
17.2
|
1.0
|
OE2
|
C:GLU42
|
3.3
|
20.8
|
1.0
|
OE1
|
C:GLN244
|
3.6
|
29.7
|
1.0
|
CE
|
C:LYS45
|
3.8
|
25.4
|
1.0
|
CD2
|
C:LEU241
|
3.8
|
15.6
|
1.0
|
CG
|
C:HIS46
|
4.0
|
15.3
|
1.0
|
ND1
|
C:HIS46
|
4.0
|
20.1
|
1.0
|
NZ
|
C:LYS45
|
4.0
|
21.0
|
1.0
|
CG
|
C:GLU42
|
4.3
|
11.5
|
1.0
|
NE2
|
C:GLN244
|
4.4
|
28.0
|
1.0
|
CD
|
C:GLN244
|
4.4
|
28.3
|
1.0
|
CD1
|
C:LEU246
|
4.6
|
26.7
|
1.0
|
CB
|
C:GLU42
|
4.6
|
10.4
|
1.0
|
|
Reference:
A.H.Ahmed,
S.Wang,
H.H.Chuang,
R.E.Oswald.
Mechanism of Ampa Receptor Activation By Partial Agonists: Disulfide Trapping of Closed Lobe Conformations. J.Biol.Chem. V. 286 35257 2011.
ISSN: ISSN 0021-9258
PubMed: 21846932
DOI: 10.1074/JBC.M111.269001
Page generated: Sat Oct 26 16:26:16 2024
|