Sodium in PDB 5h9w: Crystal Structure of Regnase Pin Domain, Form II
Protein crystallography data
The structure of Crystal Structure of Regnase Pin Domain, Form II, PDB code: 5h9w
was solved by
M.Yokogawa,
T.Tsushima,
W.Adachi,
N.N.Noda,
F.Inagaki,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
26.94 /
2.60
|
Space group
|
P 31 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
113.333,
113.333,
78.373,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
19.1 /
23.1
|
Sodium Binding Sites:
The binding sites of Sodium atom in the Crystal Structure of Regnase Pin Domain, Form II
(pdb code 5h9w). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the
Crystal Structure of Regnase Pin Domain, Form II, PDB code: 5h9w:
Jump to Sodium binding site number:
1;
2;
Sodium binding site 1 out
of 2 in 5h9w
Go back to
Sodium Binding Sites List in 5h9w
Sodium binding site 1 out
of 2 in the Crystal Structure of Regnase Pin Domain, Form II
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 1 of Crystal Structure of Regnase Pin Domain, Form II within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Na401
b:61.5
occ:1.00
|
O
|
A:HIS149
|
2.0
|
54.1
|
1.0
|
O
|
A:ASN151
|
2.2
|
45.8
|
1.0
|
O
|
A:VAL154
|
2.3
|
58.0
|
1.0
|
O
|
A:MET147
|
2.5
|
52.5
|
1.0
|
O
|
A:ALA146
|
2.6
|
58.2
|
1.0
|
C
|
A:MET147
|
3.0
|
48.8
|
1.0
|
C
|
A:HIS149
|
3.2
|
51.7
|
1.0
|
C
|
A:ASN151
|
3.4
|
54.0
|
1.0
|
CA
|
A:MET147
|
3.4
|
47.7
|
1.0
|
C
|
A:VAL154
|
3.4
|
57.3
|
1.0
|
C
|
A:ALA146
|
3.7
|
51.9
|
1.0
|
N
|
A:HIS149
|
3.8
|
50.9
|
1.0
|
CB
|
A:SER156
|
3.8
|
54.1
|
1.0
|
N
|
A:SER148
|
3.9
|
49.9
|
1.0
|
C
|
A:SER148
|
3.9
|
51.6
|
1.0
|
N
|
A:SER156
|
4.0
|
49.1
|
1.0
|
CA
|
A:LYS152
|
4.0
|
54.6
|
1.0
|
N
|
A:MET147
|
4.0
|
47.2
|
1.0
|
N
|
A:VAL154
|
4.0
|
52.5
|
1.0
|
C
|
A:GLY150
|
4.1
|
56.3
|
1.0
|
CA
|
A:HIS149
|
4.1
|
51.2
|
1.0
|
N
|
A:LYS152
|
4.1
|
54.0
|
1.0
|
N
|
A:GLY150
|
4.2
|
55.7
|
1.0
|
O
|
A:GLY150
|
4.2
|
54.7
|
1.0
|
CA
|
A:VAL154
|
4.2
|
55.1
|
1.0
|
N
|
A:ASN151
|
4.2
|
59.1
|
1.0
|
O
|
A:SER148
|
4.3
|
50.3
|
1.0
|
C
|
A:LYS152
|
4.3
|
50.8
|
1.0
|
CA
|
A:GLY150
|
4.4
|
56.2
|
1.0
|
CA
|
A:ASN151
|
4.4
|
57.4
|
1.0
|
CA
|
A:SER148
|
4.4
|
51.6
|
1.0
|
CB
|
A:VAL154
|
4.4
|
56.0
|
1.0
|
N
|
A:PHE155
|
4.5
|
58.7
|
1.0
|
CA
|
A:SER156
|
4.6
|
53.1
|
1.0
|
CB
|
A:MET147
|
4.7
|
43.7
|
1.0
|
CA
|
A:PHE155
|
4.7
|
55.7
|
1.0
|
O
|
A:LYS152
|
4.7
|
46.3
|
1.0
|
N
|
A:GLU153
|
4.7
|
52.9
|
1.0
|
C
|
A:PHE155
|
4.7
|
54.1
|
1.0
|
CB
|
A:HIS149
|
4.8
|
53.1
|
1.0
|
OG
|
A:SER156
|
5.0
|
58.4
|
1.0
|
CA
|
A:ALA146
|
5.0
|
51.3
|
1.0
|
|
Sodium binding site 2 out
of 2 in 5h9w
Go back to
Sodium Binding Sites List in 5h9w
Sodium binding site 2 out
of 2 in the Crystal Structure of Regnase Pin Domain, Form II
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 2 of Crystal Structure of Regnase Pin Domain, Form II within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Na401
b:61.7
occ:1.00
|
O
|
B:HIS149
|
2.1
|
54.6
|
1.0
|
O
|
B:VAL154
|
2.2
|
49.3
|
1.0
|
O
|
B:ASN151
|
2.2
|
55.9
|
1.0
|
O
|
B:MET147
|
2.4
|
50.0
|
1.0
|
O
|
B:ALA146
|
2.6
|
51.9
|
1.0
|
C
|
B:MET147
|
2.9
|
49.2
|
1.0
|
C
|
B:HIS149
|
3.3
|
51.4
|
1.0
|
CA
|
B:MET147
|
3.3
|
46.5
|
1.0
|
C
|
B:ASN151
|
3.4
|
64.9
|
1.0
|
C
|
B:VAL154
|
3.4
|
49.4
|
1.0
|
C
|
B:ALA146
|
3.6
|
46.1
|
1.0
|
N
|
B:HIS149
|
3.8
|
53.5
|
1.0
|
N
|
B:SER148
|
3.9
|
55.3
|
1.0
|
CB
|
B:SER156
|
3.9
|
52.3
|
1.0
|
C
|
B:SER148
|
3.9
|
54.5
|
1.0
|
N
|
B:SER156
|
4.0
|
49.5
|
1.0
|
N
|
B:MET147
|
4.0
|
46.5
|
1.0
|
C
|
B:GLY150
|
4.0
|
55.6
|
1.0
|
CA
|
B:LYS152
|
4.1
|
61.3
|
1.0
|
N
|
B:VAL154
|
4.1
|
51.7
|
1.0
|
N
|
B:LYS152
|
4.1
|
62.5
|
1.0
|
CA
|
B:HIS149
|
4.2
|
52.5
|
1.0
|
N
|
B:ASN151
|
4.2
|
57.7
|
1.0
|
CA
|
B:VAL154
|
4.2
|
49.6
|
1.0
|
O
|
B:GLY150
|
4.2
|
67.3
|
1.0
|
N
|
B:GLY150
|
4.2
|
53.3
|
1.0
|
O
|
B:SER148
|
4.3
|
60.2
|
1.0
|
C
|
B:LYS152
|
4.3
|
57.1
|
1.0
|
CA
|
B:ASN151
|
4.4
|
63.1
|
1.0
|
CA
|
B:GLY150
|
4.4
|
55.7
|
1.0
|
CA
|
B:SER148
|
4.4
|
54.4
|
1.0
|
CB
|
B:VAL154
|
4.5
|
49.3
|
1.0
|
N
|
B:PHE155
|
4.5
|
46.9
|
1.0
|
CB
|
B:MET147
|
4.6
|
46.1
|
1.0
|
CA
|
B:SER156
|
4.6
|
49.8
|
1.0
|
CA
|
B:PHE155
|
4.6
|
48.6
|
1.0
|
C
|
B:PHE155
|
4.7
|
48.7
|
1.0
|
O
|
B:LYS152
|
4.7
|
53.0
|
1.0
|
N
|
B:GLU153
|
4.8
|
59.6
|
1.0
|
CB
|
B:HIS149
|
4.9
|
52.0
|
1.0
|
CA
|
B:ALA146
|
5.0
|
47.1
|
1.0
|
CE
|
B:MET147
|
5.0
|
48.4
|
1.0
|
|
Reference:
M.Yokogawa,
T.Tsushima,
N.N.Noda,
H.Kumeta,
Y.Enokizono,
K.Yamashita,
D.M.Standley,
O.Takeuchi,
S.Akira,
F.Inagaki.
Structural Basis For the Regulation of Enzymatic Activity of Regnase-1 By Domain-Domain Interactions Sci Rep V. 6 22324 2016.
ISSN: ESSN 2045-2322
PubMed: 26927947
DOI: 10.1038/SREP22324
Page generated: Mon Oct 7 21:21:08 2024
|