Manganese in PDB 1zm8: Apo Crystal Structure of Nuclease A From Anabaena Sp.
Protein crystallography data
The structure of Apo Crystal Structure of Nuclease A From Anabaena Sp., PDB code: 1zm8
was solved by
M.Ghosh,
G.Meiss,
A.Pingoud,
R.E.London,
L.C.Pedersen,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
30.87 /
1.90
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
46.690,
66.682,
81.730,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
21.2 /
25.6
|
Other elements in 1zm8:
The structure of Apo Crystal Structure of Nuclease A From Anabaena Sp. also contains other interesting chemical elements:
Manganese Binding Sites:
The binding sites of Manganese atom in the Apo Crystal Structure of Nuclease A From Anabaena Sp.
(pdb code 1zm8). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 3 binding sites of Manganese where determined in the
Apo Crystal Structure of Nuclease A From Anabaena Sp., PDB code: 1zm8:
Jump to Manganese binding site number:
1;
2;
3;
Manganese binding site 1 out
of 3 in 1zm8
Go back to
Manganese Binding Sites List in 1zm8
Manganese binding site 1 out
of 3 in the Apo Crystal Structure of Nuclease A From Anabaena Sp.
 Mono view
 Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of Apo Crystal Structure of Nuclease A From Anabaena Sp. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn275
b:37.6
occ:1.00
|
OD1
|
A:ASN155
|
2.0
|
38.1
|
1.0
|
O
|
A:HOH282
|
2.1
|
31.3
|
1.0
|
O4
|
A:SO4278
|
2.1
|
59.5
|
1.0
|
O
|
A:HOH281
|
2.2
|
30.4
|
1.0
|
O
|
A:HOH284
|
2.3
|
29.6
|
1.0
|
O
|
A:HOH283
|
2.4
|
35.6
|
1.0
|
CG
|
A:ASN155
|
3.2
|
36.7
|
1.0
|
S
|
A:SO4278
|
3.4
|
61.0
|
1.0
|
ND2
|
A:ASN155
|
3.7
|
35.6
|
1.0
|
O2
|
A:SO4278
|
3.8
|
60.0
|
1.0
|
O3
|
A:SO4278
|
3.8
|
59.9
|
1.0
|
N
|
A:HIS124
|
4.0
|
34.8
|
1.0
|
O
|
A:HOH300
|
4.1
|
32.0
|
1.0
|
OE1
|
A:GLU163
|
4.1
|
34.6
|
1.0
|
OE2
|
A:GLU163
|
4.1
|
32.2
|
1.0
|
ND1
|
A:HIS124
|
4.3
|
34.0
|
1.0
|
OE1
|
A:GLN150
|
4.3
|
42.7
|
1.0
|
O
|
A:ASN155
|
4.4
|
37.1
|
1.0
|
CB
|
A:ASN155
|
4.4
|
36.3
|
1.0
|
CD1
|
A:TRP159
|
4.5
|
34.6
|
1.0
|
CB
|
A:HIS124
|
4.5
|
33.5
|
1.0
|
CA
|
A:GLY123
|
4.5
|
36.8
|
1.0
|
CD
|
A:GLU163
|
4.5
|
32.6
|
1.0
|
O
|
A:HIS124
|
4.5
|
32.1
|
1.0
|
O1
|
A:SO4278
|
4.5
|
63.3
|
1.0
|
CA
|
A:ASN155
|
4.7
|
37.3
|
1.0
|
C
|
A:GLY123
|
4.7
|
36.9
|
1.0
|
CA
|
A:HIS124
|
4.8
|
33.4
|
1.0
|
C
|
A:ASN155
|
4.8
|
37.9
|
1.0
|
CG
|
A:HIS124
|
4.8
|
33.5
|
1.0
|
NE1
|
A:TRP159
|
4.9
|
34.3
|
1.0
|
|
Manganese binding site 2 out
of 3 in 1zm8
Go back to
Manganese Binding Sites List in 1zm8
Manganese binding site 2 out
of 3 in the Apo Crystal Structure of Nuclease A From Anabaena Sp.
 Mono view
 Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of Apo Crystal Structure of Nuclease A From Anabaena Sp. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn276
b:39.7
occ:1.00
|
OD1
|
A:ASP246
|
2.1
|
27.7
|
0.7
|
OE1
|
A:GLU249
|
2.1
|
35.4
|
1.0
|
OE1
|
A:GLU269
|
2.1
|
39.8
|
1.0
|
O
|
A:HOH285
|
2.4
|
46.2
|
1.0
|
CD
|
A:GLU249
|
3.1
|
36.1
|
1.0
|
CD
|
A:GLU269
|
3.3
|
43.0
|
1.0
|
CG
|
A:ASP246
|
3.3
|
29.8
|
0.7
|
OE2
|
A:GLU249
|
3.5
|
34.3
|
1.0
|
CB
|
A:GLU269
|
3.6
|
43.2
|
1.0
|
MN
|
A:MN277
|
3.7
|
42.9
|
1.0
|
CG
|
A:GLU269
|
4.0
|
41.9
|
1.0
|
OD2
|
A:ASP246
|
4.0
|
30.4
|
0.7
|
O
|
A:HOH325
|
4.1
|
39.3
|
1.0
|
OE2
|
A:GLU269
|
4.3
|
41.1
|
1.0
|
CA
|
A:ASP246
|
4.3
|
32.3
|
1.0
|
CB
|
A:ASP246
|
4.4
|
30.8
|
0.7
|
CG
|
A:GLU249
|
4.4
|
35.0
|
1.0
|
N
|
A:ASP246
|
4.7
|
32.7
|
1.0
|
CA
|
A:GLU269
|
4.9
|
43.9
|
1.0
|
OE1
|
A:GLN265
|
5.0
|
36.8
|
1.0
|
|
Manganese binding site 3 out
of 3 in 1zm8
Go back to
Manganese Binding Sites List in 1zm8
Manganese binding site 3 out
of 3 in the Apo Crystal Structure of Nuclease A From Anabaena Sp.
 Mono view
 Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 3 of Apo Crystal Structure of Nuclease A From Anabaena Sp. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn277
b:42.9
occ:1.00
|
OD1
|
A:ASP255
|
2.4
|
36.4
|
1.0
|
OE2
|
A:GLU249
|
2.4
|
34.3
|
1.0
|
O
|
A:PHE256
|
2.5
|
32.8
|
1.0
|
OE1
|
A:GLN265
|
2.5
|
36.8
|
1.0
|
OE1
|
A:GLU269
|
2.5
|
39.8
|
1.0
|
OE2
|
A:GLU269
|
2.7
|
41.1
|
1.0
|
CD
|
A:GLU269
|
2.9
|
43.0
|
1.0
|
CD
|
A:GLU249
|
3.5
|
36.1
|
1.0
|
C
|
A:PHE256
|
3.6
|
33.1
|
1.0
|
N
|
A:PHE256
|
3.6
|
30.9
|
1.0
|
CG
|
A:ASP255
|
3.6
|
34.9
|
1.0
|
CD
|
A:GLN265
|
3.6
|
39.0
|
1.0
|
MN
|
A:MN276
|
3.7
|
39.7
|
1.0
|
OE1
|
A:GLU249
|
3.8
|
35.4
|
1.0
|
C
|
A:ASP255
|
4.0
|
31.6
|
1.0
|
CA
|
A:PHE256
|
4.1
|
30.9
|
1.0
|
CA
|
A:ASP255
|
4.3
|
31.9
|
1.0
|
CG
|
A:GLN265
|
4.4
|
41.2
|
1.0
|
OD2
|
A:ASP255
|
4.4
|
33.8
|
1.0
|
CG
|
A:GLU269
|
4.4
|
41.9
|
1.0
|
CB
|
A:ASP255
|
4.5
|
31.4
|
1.0
|
NE2
|
A:GLN265
|
4.6
|
36.3
|
1.0
|
O
|
A:HOH310
|
4.7
|
35.1
|
1.0
|
N
|
A:LEU257
|
4.7
|
32.2
|
1.0
|
C
|
A:LEU257
|
4.7
|
35.5
|
1.0
|
O
|
A:ASP255
|
4.8
|
30.1
|
1.0
|
CB
|
A:PHE256
|
4.8
|
31.0
|
1.0
|
CG
|
A:GLU249
|
4.8
|
35.0
|
1.0
|
CB
|
A:GLN265
|
4.8
|
42.6
|
1.0
|
O
|
A:LEU257
|
4.8
|
36.8
|
1.0
|
O
|
A:HOH285
|
4.8
|
46.2
|
1.0
|
CB
|
A:LEU257
|
4.9
|
35.0
|
1.0
|
N
|
A:SER258
|
4.9
|
36.9
|
1.0
|
|
Reference:
M.Ghosh,
G.Meiss,
A.Pingoud,
R.E.London,
L.C.Pedersen.
Structural Insights Into the Mechanism of Nuclease A, A Beta Beta Alpha Metal Nuclease From Anabaena. J.Biol.Chem. V. 280 27990 2005.
ISSN: ISSN 0021-9258
PubMed: 15897201
DOI: 10.1074/JBC.M501798200
Page generated: Sat Oct 5 13:17:48 2024
|