Sodium in PDB 7ndk: Crystal Structure of ZC3H12C Pin Catalytic Mutant
Protein crystallography data
The structure of Crystal Structure of ZC3H12C Pin Catalytic Mutant, PDB code: 7ndk
was solved by
A.Garg,
U.Heinemann,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
38.75 /
2.34
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
38.753,
61.475,
111.62,
90,
90.06,
90
|
R / Rfree (%)
|
22.9 /
27.5
|
Sodium Binding Sites:
The binding sites of Sodium atom in the Crystal Structure of ZC3H12C Pin Catalytic Mutant
(pdb code 7ndk). 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 ZC3H12C Pin Catalytic Mutant, PDB code: 7ndk:
Jump to Sodium binding site number:
1;
2;
Sodium binding site 1 out
of 2 in 7ndk
Go back to
Sodium Binding Sites List in 7ndk
Sodium binding site 1 out
of 2 in the Crystal Structure of ZC3H12C Pin Catalytic Mutant
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 ZC3H12C Pin Catalytic Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Na501
b:43.0
occ:1.00
|
O
|
B:ASN281
|
2.2
|
47.6
|
1.0
|
O
|
B:VAL284
|
2.2
|
54.9
|
1.0
|
O
|
B:HIS279
|
2.5
|
54.9
|
1.0
|
O
|
B:ALA276
|
2.9
|
43.6
|
1.0
|
O
|
B:MET277
|
2.9
|
45.0
|
1.0
|
C
|
B:MET277
|
3.3
|
45.3
|
1.0
|
C
|
B:ASN281
|
3.4
|
56.0
|
1.0
|
C
|
B:VAL284
|
3.4
|
57.4
|
1.0
|
C
|
B:HIS279
|
3.5
|
54.9
|
1.0
|
CA
|
B:MET277
|
3.7
|
42.2
|
1.0
|
CB
|
B:SER286
|
3.8
|
54.9
|
1.0
|
N
|
B:HIS279
|
3.9
|
52.4
|
1.0
|
C
|
B:ALA276
|
3.9
|
41.3
|
1.0
|
CG2
|
B:VAL284
|
4.0
|
55.2
|
1.0
|
N
|
B:SER286
|
4.0
|
56.8
|
1.0
|
N
|
B:ASN281
|
4.0
|
57.0
|
1.0
|
C
|
B:GLY280
|
4.2
|
58.2
|
1.0
|
N
|
B:SER278
|
4.2
|
45.5
|
1.0
|
CA
|
B:ASN281
|
4.2
|
57.5
|
1.0
|
C
|
B:SER278
|
4.2
|
48.9
|
1.0
|
N
|
B:VAL284
|
4.2
|
56.2
|
1.0
|
N
|
B:MET277
|
4.2
|
43.2
|
1.0
|
CA
|
B:HIS279
|
4.3
|
55.1
|
1.0
|
N
|
B:LYS282
|
4.3
|
57.7
|
1.0
|
CA
|
B:VAL284
|
4.3
|
56.7
|
1.0
|
CA
|
B:LYS282
|
4.3
|
59.5
|
1.0
|
N
|
B:PHE285
|
4.4
|
55.5
|
1.0
|
N
|
B:GLY280
|
4.4
|
54.0
|
1.0
|
O
|
B:GLY280
|
4.5
|
56.7
|
1.0
|
CA
|
B:SER286
|
4.6
|
53.9
|
1.0
|
CA
|
B:PHE285
|
4.6
|
56.4
|
1.0
|
CA
|
B:GLY280
|
4.6
|
57.4
|
1.0
|
C
|
B:PHE285
|
4.7
|
57.2
|
1.0
|
C
|
B:LYS282
|
4.7
|
62.5
|
1.0
|
CA
|
B:SER278
|
4.7
|
46.8
|
1.0
|
O
|
B:SER278
|
4.7
|
50.3
|
1.0
|
CB
|
B:ASN281
|
4.7
|
58.5
|
1.0
|
CB
|
B:VAL284
|
4.8
|
54.9
|
1.0
|
CB
|
B:HIS279
|
4.9
|
57.8
|
1.0
|
CE
|
B:MET277
|
4.9
|
39.8
|
1.0
|
CB
|
B:MET277
|
5.0
|
42.3
|
1.0
|
OG
|
B:SER286
|
5.0
|
56.6
|
1.0
|
|
Sodium binding site 2 out
of 2 in 7ndk
Go back to
Sodium Binding Sites List in 7ndk
Sodium binding site 2 out
of 2 in the Crystal Structure of ZC3H12C Pin Catalytic Mutant
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 ZC3H12C Pin Catalytic Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Na501
b:39.5
occ:1.00
|
O
|
D:ASN281
|
2.2
|
53.9
|
1.0
|
O
|
D:VAL284
|
2.3
|
53.3
|
1.0
|
O
|
D:HIS279
|
2.4
|
64.3
|
1.0
|
O
|
D:MET277
|
2.6
|
52.4
|
1.0
|
O
|
D:ALA276
|
2.7
|
54.4
|
1.0
|
C
|
D:MET277
|
3.1
|
51.2
|
1.0
|
C
|
D:ASN281
|
3.4
|
60.5
|
1.0
|
C
|
D:VAL284
|
3.4
|
52.2
|
1.0
|
CA
|
D:MET277
|
3.5
|
50.3
|
1.0
|
C
|
D:HIS279
|
3.5
|
64.4
|
1.0
|
CG2
|
D:VAL284
|
3.6
|
51.0
|
1.0
|
C
|
D:ALA276
|
3.8
|
52.9
|
1.0
|
N
|
D:VAL284
|
3.8
|
53.9
|
1.0
|
N
|
D:ASN281
|
3.9
|
62.5
|
1.0
|
N
|
D:HIS279
|
4.0
|
54.2
|
1.0
|
CA
|
D:VAL284
|
4.0
|
51.2
|
1.0
|
N
|
D:SER278
|
4.0
|
52.8
|
1.0
|
C
|
D:GLY280
|
4.1
|
62.0
|
1.0
|
N
|
D:MET277
|
4.1
|
53.1
|
1.0
|
N
|
D:SER286
|
4.2
|
57.2
|
1.0
|
CB
|
D:SER286
|
4.2
|
55.9
|
1.0
|
CA
|
D:ASN281
|
4.2
|
60.9
|
1.0
|
C
|
D:LYS282
|
4.3
|
65.3
|
1.0
|
N
|
D:LYS282
|
4.3
|
64.3
|
1.0
|
C
|
D:SER278
|
4.4
|
52.5
|
1.0
|
CA
|
D:HIS279
|
4.4
|
62.0
|
1.0
|
N
|
D:GLY280
|
4.4
|
64.4
|
1.0
|
CB
|
D:VAL284
|
4.4
|
50.8
|
1.0
|
CA
|
D:GLY280
|
4.4
|
61.9
|
1.0
|
CA
|
D:LYS282
|
4.5
|
66.8
|
1.0
|
N
|
D:PHE285
|
4.5
|
52.3
|
1.0
|
N
|
D:GLU283
|
4.5
|
62.6
|
1.0
|
CA
|
D:SER278
|
4.6
|
49.9
|
1.0
|
O
|
D:LYS282
|
4.6
|
68.6
|
1.0
|
O
|
D:GLY280
|
4.6
|
59.0
|
1.0
|
CB
|
D:MET277
|
4.7
|
49.8
|
1.0
|
C
|
D:GLU283
|
4.8
|
58.5
|
1.0
|
CA
|
D:SER286
|
4.8
|
56.6
|
1.0
|
CA
|
D:PHE285
|
4.8
|
54.0
|
1.0
|
CE
|
D:MET277
|
4.9
|
53.7
|
1.0
|
CB
|
D:ASN281
|
5.0
|
61.3
|
1.0
|
SD
|
D:MET277
|
5.0
|
53.5
|
1.0
|
|
Reference:
A.Garg,
Y.Roske,
S.Yamada,
T.Uehata,
O.Takeuchi,
U.Heinemann.
Pin and Ccch Zn-Finger Domains Coordinate Rna Targeting in ZC3H12 Family Endoribonucleases. Nucleic Acids Res. 2021.
ISSN: ESSN 1362-4962
PubMed: 33950203
DOI: 10.1093/NAR/GKAB316
Page generated: Tue Oct 8 18:09:04 2024
|