Copper in PDB 2xla: Structure and Metal-Loading of A Soluble Periplasm Cupro-Protein: Cu- Cuca-Closed
Protein crystallography data
The structure of Structure and Metal-Loading of A Soluble Periplasm Cupro-Protein: Cu- Cuca-Closed, PDB code: 2xla
was solved by
K.J.Waldron,
S.J.Firbank,
S.J.Dainty,
M.Perez-Rama,
S.Tottey,
N.J.Robinson,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
37.42 /
1.93
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
50.310,
72.510,
262.100,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
16.1 /
20.3
|
Copper Binding Sites:
The binding sites of Copper atom in the Structure and Metal-Loading of A Soluble Periplasm Cupro-Protein: Cu- Cuca-Closed
(pdb code 2xla). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the
Structure and Metal-Loading of A Soluble Periplasm Cupro-Protein: Cu- Cuca-Closed, PDB code: 2xla:
Jump to Copper binding site number:
1;
2;
3;
4;
Copper binding site 1 out
of 4 in 2xla
Go back to
Copper Binding Sites List in 2xla
Copper binding site 1 out
of 4 in the Structure and Metal-Loading of A Soluble Periplasm Cupro-Protein: Cu- Cuca-Closed
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of Structure and Metal-Loading of A Soluble Periplasm Cupro-Protein: Cu- Cuca-Closed within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu1298
b:4.9
occ:1.00
|
NE2
|
A:HIS119
|
2.1
|
5.1
|
1.0
|
NE2
|
A:HIS117
|
2.1
|
4.2
|
1.0
|
OE1
|
A:GLU124
|
2.1
|
12.0
|
1.0
|
NE2
|
A:HIS178
|
2.2
|
9.7
|
1.0
|
O
|
A:HOH2318
|
2.2
|
25.3
|
1.0
|
O
|
A:HOH2080
|
2.7
|
25.8
|
1.0
|
CD2
|
A:HIS119
|
2.9
|
4.2
|
1.0
|
CD2
|
A:HIS117
|
3.0
|
5.6
|
1.0
|
CD
|
A:GLU124
|
3.1
|
8.5
|
1.0
|
CD2
|
A:HIS178
|
3.1
|
7.9
|
1.0
|
CE1
|
A:HIS119
|
3.1
|
8.2
|
1.0
|
CE1
|
A:HIS117
|
3.2
|
8.4
|
1.0
|
CE1
|
A:HIS178
|
3.2
|
10.1
|
1.0
|
OE2
|
A:GLU124
|
3.4
|
9.0
|
1.0
|
O
|
A:HOH2319
|
3.9
|
18.4
|
1.0
|
CG
|
A:HIS119
|
4.1
|
5.3
|
1.0
|
CG
|
A:HIS117
|
4.2
|
5.9
|
1.0
|
ND1
|
A:HIS119
|
4.2
|
6.4
|
1.0
|
N2
|
A:URE1299
|
4.2
|
13.6
|
1.0
|
ND1
|
A:HIS117
|
4.2
|
7.0
|
1.0
|
ND1
|
A:HIS178
|
4.3
|
9.9
|
1.0
|
CG
|
A:HIS178
|
4.3
|
8.7
|
1.0
|
CG
|
A:GLU124
|
4.5
|
6.0
|
1.0
|
CZ
|
A:PHE126
|
4.5
|
8.7
|
1.0
|
NE1
|
A:TRP194
|
4.7
|
9.6
|
1.0
|
CB
|
A:GLU124
|
4.8
|
4.0
|
1.0
|
CE1
|
A:PHE126
|
5.0
|
7.8
|
1.0
|
|
Copper binding site 2 out
of 4 in 2xla
Go back to
Copper Binding Sites List in 2xla
Copper binding site 2 out
of 4 in the Structure and Metal-Loading of A Soluble Periplasm Cupro-Protein: Cu- Cuca-Closed
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of Structure and Metal-Loading of A Soluble Periplasm Cupro-Protein: Cu- Cuca-Closed within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu1298
b:6.0
occ:1.00
|
NE2
|
B:HIS119
|
2.1
|
9.4
|
1.0
|
NE2
|
B:HIS117
|
2.1
|
6.4
|
1.0
|
NE2
|
B:HIS178
|
2.2
|
12.8
|
1.0
|
OE1
|
B:GLU124
|
2.2
|
13.5
|
1.0
|
O
|
B:HOH2247
|
2.3
|
20.1
|
1.0
|
CD2
|
B:HIS119
|
3.0
|
8.6
|
1.0
|
CD2
|
B:HIS117
|
3.0
|
7.7
|
1.0
|
CE1
|
B:HIS117
|
3.1
|
8.3
|
1.0
|
CE1
|
B:HIS178
|
3.1
|
13.3
|
1.0
|
CE1
|
B:HIS119
|
3.2
|
8.1
|
1.0
|
CD
|
B:GLU124
|
3.2
|
10.7
|
1.0
|
CD2
|
B:HIS178
|
3.2
|
11.7
|
1.0
|
O
|
B:HOH2058
|
3.2
|
35.0
|
1.0
|
OE2
|
B:GLU124
|
3.5
|
14.2
|
1.0
|
O
|
B:HOH2246
|
3.8
|
19.0
|
1.0
|
CG
|
B:HIS119
|
4.2
|
8.3
|
1.0
|
CG
|
B:HIS117
|
4.2
|
6.0
|
1.0
|
ND1
|
B:HIS117
|
4.2
|
6.5
|
1.0
|
ND1
|
B:HIS119
|
4.2
|
9.6
|
1.0
|
ND1
|
B:HIS178
|
4.3
|
12.1
|
1.0
|
CG
|
B:HIS178
|
4.3
|
8.8
|
1.0
|
NE1
|
B:TRP194
|
4.4
|
8.8
|
1.0
|
CZ
|
B:PHE126
|
4.4
|
7.4
|
1.0
|
N2
|
B:URE1299
|
4.5
|
15.2
|
1.0
|
CG
|
B:GLU124
|
4.5
|
7.5
|
1.0
|
CB
|
B:GLU124
|
4.8
|
6.7
|
1.0
|
CD1
|
B:TRP194
|
4.8
|
7.9
|
1.0
|
CE1
|
B:PHE126
|
4.9
|
8.7
|
1.0
|
|
Copper binding site 3 out
of 4 in 2xla
Go back to
Copper Binding Sites List in 2xla
Copper binding site 3 out
of 4 in the Structure and Metal-Loading of A Soluble Periplasm Cupro-Protein: Cu- Cuca-Closed
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of Structure and Metal-Loading of A Soluble Periplasm Cupro-Protein: Cu- Cuca-Closed within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Cu1298
b:7.6
occ:1.00
|
NE2
|
C:HIS119
|
2.0
|
8.9
|
1.0
|
NE2
|
C:HIS117
|
2.1
|
11.4
|
1.0
|
NE2
|
C:HIS178
|
2.1
|
12.7
|
1.0
|
OE1
|
C:GLU124
|
2.2
|
12.9
|
1.0
|
O
|
C:HOH2279
|
2.4
|
21.2
|
1.0
|
O
|
C:HOH2071
|
2.5
|
26.1
|
1.0
|
CD2
|
C:HIS119
|
2.9
|
5.4
|
1.0
|
CD2
|
C:HIS117
|
3.0
|
10.7
|
1.0
|
CE1
|
C:HIS178
|
3.0
|
13.2
|
1.0
|
CD2
|
C:HIS178
|
3.1
|
11.4
|
1.0
|
CE1
|
C:HIS117
|
3.1
|
11.8
|
1.0
|
CE1
|
C:HIS119
|
3.1
|
7.8
|
1.0
|
CD
|
C:GLU124
|
3.2
|
11.9
|
1.0
|
OE2
|
C:GLU124
|
3.5
|
16.3
|
1.0
|
O
|
C:HOH2278
|
3.9
|
18.8
|
1.0
|
CG
|
C:HIS119
|
4.1
|
7.3
|
1.0
|
CG
|
C:HIS117
|
4.1
|
10.0
|
1.0
|
ND1
|
C:HIS117
|
4.2
|
10.8
|
1.0
|
ND1
|
C:HIS178
|
4.2
|
13.5
|
1.0
|
ND1
|
C:HIS119
|
4.2
|
7.6
|
1.0
|
CG
|
C:HIS178
|
4.2
|
10.9
|
1.0
|
N1
|
C:URE1299
|
4.3
|
18.2
|
1.0
|
NE1
|
C:TRP194
|
4.5
|
8.4
|
1.0
|
CG
|
C:GLU124
|
4.5
|
9.6
|
1.0
|
CZ
|
C:PHE126
|
4.5
|
13.6
|
1.0
|
CB
|
C:GLU124
|
4.8
|
8.6
|
1.0
|
CD1
|
C:TRP194
|
4.9
|
8.8
|
1.0
|
CE1
|
C:PHE126
|
5.0
|
13.0
|
1.0
|
|
Copper binding site 4 out
of 4 in 2xla
Go back to
Copper Binding Sites List in 2xla
Copper binding site 4 out
of 4 in the Structure and Metal-Loading of A Soluble Periplasm Cupro-Protein: Cu- Cuca-Closed
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 4 of Structure and Metal-Loading of A Soluble Periplasm Cupro-Protein: Cu- Cuca-Closed within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Cu1298
b:7.8
occ:1.00
|
O
|
D:HOH2047
|
1.9
|
33.8
|
1.0
|
NE2
|
D:HIS117
|
2.1
|
10.8
|
1.0
|
NE2
|
D:HIS119
|
2.1
|
8.2
|
1.0
|
OE1
|
D:GLU124
|
2.2
|
12.6
|
1.0
|
NE2
|
D:HIS178
|
2.2
|
13.7
|
1.0
|
CD2
|
D:HIS119
|
2.9
|
9.8
|
1.0
|
CD2
|
D:HIS117
|
3.0
|
11.0
|
1.0
|
CE1
|
D:HIS117
|
3.1
|
10.5
|
1.0
|
CD2
|
D:HIS178
|
3.1
|
9.9
|
1.0
|
CE1
|
D:HIS119
|
3.2
|
9.9
|
1.0
|
CD
|
D:GLU124
|
3.2
|
15.1
|
1.0
|
CE1
|
D:HIS178
|
3.2
|
13.6
|
1.0
|
OE2
|
D:GLU124
|
3.5
|
18.9
|
1.0
|
O
|
D:HOH2228
|
3.9
|
22.5
|
1.0
|
CG
|
D:HIS119
|
4.1
|
10.2
|
1.0
|
CG
|
D:HIS117
|
4.1
|
8.7
|
1.0
|
ND1
|
D:HIS117
|
4.1
|
9.6
|
1.0
|
ND1
|
D:HIS119
|
4.2
|
9.3
|
1.0
|
CG
|
D:HIS178
|
4.3
|
10.7
|
1.0
|
ND1
|
D:HIS178
|
4.3
|
14.4
|
1.0
|
N1
|
D:URE1299
|
4.4
|
17.8
|
1.0
|
NE1
|
D:TRP194
|
4.6
|
11.2
|
1.0
|
CG
|
D:GLU124
|
4.6
|
12.8
|
1.0
|
CZ
|
D:PHE126
|
4.6
|
14.0
|
1.0
|
CB
|
D:GLU124
|
4.8
|
12.2
|
1.0
|
|
Reference:
K.J.Waldron,
S.J.Firbank,
S.J.Dainty,
M.Perez-Rama,
S.Tottey,
N.J.Robinson.
Structure and Metal Loading of A Soluble Periplasm Cuproprotein. J.Biol.Chem. V. 285 32504 2010.
ISSN: ISSN 0021-9258
PubMed: 20702411
DOI: 10.1074/JBC.M110.153080
Page generated: Wed Jul 31 00:10:32 2024
|