Potassium in PDB 5yew: Structural Basis For Gtp Hydrolysis and Conformational Change of Mitofusin 1 in Mediating Mitochondrial Fusion
Protein crystallography data
The structure of Structural Basis For Gtp Hydrolysis and Conformational Change of Mitofusin 1 in Mediating Mitochondrial Fusion, PDB code: 5yew
was solved by
L.Yan,
Y.Qi,
X.Huang,
C.Yu,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
50.00 /
3.20
|
Space group
|
P 32 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
207.942,
207.942,
107.893,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
22.3 /
25.7
|
Other elements in 5yew:
The structure of Structural Basis For Gtp Hydrolysis and Conformational Change of Mitofusin 1 in Mediating Mitochondrial Fusion also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Structural Basis For Gtp Hydrolysis and Conformational Change of Mitofusin 1 in Mediating Mitochondrial Fusion
(pdb code 5yew). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 3 binding sites of Potassium where determined in the
Structural Basis For Gtp Hydrolysis and Conformational Change of Mitofusin 1 in Mediating Mitochondrial Fusion, PDB code: 5yew:
Jump to Potassium binding site number:
1;
2;
3;
Potassium binding site 1 out
of 3 in 5yew
Go back to
Potassium Binding Sites List in 5yew
Potassium binding site 1 out
of 3 in the Structural Basis For Gtp Hydrolysis and Conformational Change of Mitofusin 1 in Mediating Mitochondrial Fusion
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of Structural Basis For Gtp Hydrolysis and Conformational Change of Mitofusin 1 in Mediating Mitochondrial Fusion within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K803
b:70.3
occ:1.00
|
F3
|
A:BEF802
|
2.2
|
64.5
|
1.0
|
O
|
A:GLY104
|
2.6
|
60.5
|
1.0
|
O
|
A:GLY106
|
2.7
|
48.5
|
1.0
|
OG
|
A:SER85
|
2.8
|
68.9
|
1.0
|
O3B
|
A:GDP801
|
2.9
|
65.9
|
1.0
|
O3A
|
A:GDP801
|
3.0
|
75.3
|
1.0
|
O5'
|
A:GDP801
|
3.2
|
54.9
|
1.0
|
BE
|
A:BEF802
|
3.5
|
59.7
|
1.0
|
PB
|
A:GDP801
|
3.6
|
78.6
|
1.0
|
PA
|
A:GDP801
|
3.7
|
65.0
|
1.0
|
C
|
A:GLY104
|
3.8
|
59.8
|
1.0
|
CB
|
A:SER85
|
3.9
|
65.2
|
1.0
|
CA
|
A:SER85
|
3.9
|
60.4
|
1.0
|
C
|
A:GLY106
|
4.0
|
49.1
|
1.0
|
N
|
A:SER85
|
4.1
|
59.9
|
1.0
|
CB
|
A:ILE108
|
4.1
|
64.0
|
1.0
|
F1
|
A:BEF802
|
4.1
|
69.9
|
1.0
|
N
|
A:ILE108
|
4.3
|
63.4
|
1.0
|
C5'
|
A:GDP801
|
4.4
|
52.9
|
1.0
|
CG1
|
A:ILE108
|
4.4
|
63.1
|
1.0
|
N
|
A:GLY106
|
4.5
|
47.4
|
1.0
|
N
|
A:GLY104
|
4.5
|
67.2
|
1.0
|
O2A
|
A:GDP801
|
4.5
|
77.1
|
1.0
|
C
|
A:ILE105
|
4.5
|
51.5
|
1.0
|
O2B
|
A:GDP801
|
4.6
|
45.1
|
1.0
|
CG2
|
A:THR84
|
4.6
|
61.6
|
1.0
|
CD1
|
A:ILE108
|
4.7
|
60.5
|
1.0
|
N
|
A:ILE105
|
4.7
|
56.1
|
1.0
|
CA
|
A:ILE105
|
4.7
|
52.0
|
1.0
|
O1B
|
A:GDP801
|
4.7
|
89.9
|
1.0
|
CA
|
A:GLY104
|
4.8
|
65.4
|
1.0
|
CA
|
A:HIS107
|
4.8
|
50.8
|
1.0
|
C4'
|
A:GDP801
|
4.8
|
55.9
|
1.0
|
O1A
|
A:GDP801
|
4.8
|
70.0
|
1.0
|
CA
|
A:ILE108
|
4.8
|
63.7
|
1.0
|
N
|
A:HIS107
|
4.8
|
48.8
|
1.0
|
CA
|
A:GLY106
|
4.9
|
47.4
|
1.0
|
C
|
A:HIS107
|
4.9
|
58.4
|
1.0
|
F2
|
A:BEF802
|
4.9
|
53.5
|
1.0
|
O
|
B:GLU209
|
4.9
|
47.7
|
1.0
|
O
|
A:ILE105
|
4.9
|
59.5
|
1.0
|
C
|
A:THR84
|
5.0
|
55.4
|
1.0
|
|
Potassium binding site 2 out
of 3 in 5yew
Go back to
Potassium Binding Sites List in 5yew
Potassium binding site 2 out
of 3 in the Structural Basis For Gtp Hydrolysis and Conformational Change of Mitofusin 1 in Mediating Mitochondrial Fusion
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of Structural Basis For Gtp Hydrolysis and Conformational Change of Mitofusin 1 in Mediating Mitochondrial Fusion within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K803
b:78.7
occ:1.00
|
F1
|
B:BEF802
|
2.2
|
99.4
|
1.0
|
O
|
B:GLY106
|
2.7
|
62.1
|
1.0
|
O
|
B:GLY104
|
2.7
|
60.9
|
1.0
|
O3B
|
B:GDP801
|
2.8
|
73.5
|
1.0
|
OG
|
B:SER85
|
2.9
|
70.2
|
1.0
|
O1A
|
B:GDP801
|
3.3
|
63.5
|
1.0
|
O3A
|
B:GDP801
|
3.5
|
61.7
|
1.0
|
PB
|
B:GDP801
|
3.7
|
66.2
|
1.0
|
BE
|
B:BEF802
|
3.9
|
76.0
|
1.0
|
C
|
B:GLY106
|
3.9
|
63.3
|
1.0
|
C
|
B:GLY104
|
4.0
|
69.5
|
1.0
|
CB
|
B:SER85
|
4.0
|
70.9
|
1.0
|
CA
|
B:SER85
|
4.0
|
68.4
|
1.0
|
CB
|
B:ILE108
|
4.0
|
79.4
|
1.0
|
PA
|
B:GDP801
|
4.0
|
57.6
|
1.0
|
C5'
|
B:GDP801
|
4.0
|
69.8
|
1.0
|
N
|
B:SER85
|
4.1
|
63.8
|
1.0
|
N
|
B:ILE108
|
4.1
|
68.5
|
1.0
|
CG1
|
B:ILE108
|
4.4
|
84.7
|
1.0
|
O2B
|
B:GDP801
|
4.4
|
57.1
|
1.0
|
CG2
|
B:THR84
|
4.5
|
62.3
|
1.0
|
N
|
B:GLY106
|
4.5
|
62.5
|
1.0
|
O5'
|
B:GDP801
|
4.5
|
69.8
|
1.0
|
C
|
B:ILE105
|
4.6
|
65.2
|
1.0
|
N
|
B:GLY104
|
4.6
|
75.8
|
1.0
|
CD1
|
B:ILE108
|
4.7
|
86.7
|
1.0
|
CA
|
B:HIS107
|
4.7
|
65.0
|
1.0
|
CA
|
B:ILE108
|
4.7
|
77.5
|
1.0
|
C
|
B:HIS107
|
4.7
|
67.5
|
1.0
|
N
|
B:HIS107
|
4.7
|
67.6
|
1.0
|
CA
|
B:ILE105
|
4.8
|
69.5
|
1.0
|
MG
|
B:MG804
|
4.8
|
46.2
|
1.0
|
N
|
B:ILE105
|
4.8
|
68.7
|
1.0
|
F2
|
B:BEF802
|
4.8
|
76.3
|
1.0
|
CA
|
B:GLY106
|
4.9
|
60.7
|
1.0
|
CA
|
B:GLY104
|
4.9
|
70.2
|
1.0
|
C
|
B:THR84
|
4.9
|
58.0
|
1.0
|
O
|
A:GLU209
|
4.9
|
62.6
|
1.0
|
O
|
B:ILE105
|
5.0
|
64.3
|
1.0
|
O1B
|
B:GDP801
|
5.0
|
87.4
|
1.0
|
|
Potassium binding site 3 out
of 3 in 5yew
Go back to
Potassium Binding Sites List in 5yew
Potassium binding site 3 out
of 3 in the Structural Basis For Gtp Hydrolysis and Conformational Change of Mitofusin 1 in Mediating Mitochondrial Fusion
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 3 of Structural Basis For Gtp Hydrolysis and Conformational Change of Mitofusin 1 in Mediating Mitochondrial Fusion within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K803
b:65.5
occ:1.00
|
F1
|
C:BEF802
|
2.6
|
48.9
|
1.0
|
O
|
C:GLY106
|
2.8
|
45.0
|
1.0
|
O
|
C:GLY104
|
2.9
|
49.2
|
1.0
|
O3B
|
C:GDP801
|
2.9
|
60.1
|
1.0
|
OG
|
C:SER85
|
3.0
|
58.5
|
1.0
|
O3A
|
C:GDP801
|
3.1
|
57.8
|
1.0
|
O1A
|
C:GDP801
|
3.6
|
68.0
|
1.0
|
PB
|
C:GDP801
|
3.7
|
60.2
|
1.0
|
PA
|
C:GDP801
|
3.8
|
56.1
|
1.0
|
O5'
|
C:GDP801
|
3.8
|
52.8
|
1.0
|
BE
|
C:BEF802
|
3.9
|
57.3
|
1.0
|
CA
|
C:SER85
|
4.0
|
52.2
|
1.0
|
N
|
C:SER85
|
4.0
|
47.8
|
1.0
|
CB
|
C:SER85
|
4.0
|
55.0
|
1.0
|
C
|
C:GLY106
|
4.1
|
46.2
|
1.0
|
CB
|
C:ILE108
|
4.1
|
53.2
|
1.0
|
N
|
C:ILE108
|
4.1
|
51.9
|
1.0
|
C
|
C:GLY104
|
4.2
|
57.5
|
1.0
|
C5'
|
C:GDP801
|
4.4
|
53.3
|
1.0
|
CG2
|
C:THR84
|
4.4
|
44.9
|
1.0
|
O1B
|
C:GDP801
|
4.5
|
77.8
|
1.0
|
CG1
|
C:ILE108
|
4.5
|
54.0
|
1.0
|
MG
|
C:MG804
|
4.5
|
37.4
|
1.0
|
N
|
C:GLY104
|
4.7
|
61.9
|
1.0
|
CA
|
C:HIS107
|
4.7
|
44.4
|
1.0
|
CA
|
C:ILE108
|
4.7
|
53.4
|
1.0
|
N
|
C:GLY106
|
4.7
|
46.6
|
1.0
|
C
|
C:HIS107
|
4.8
|
48.8
|
1.0
|
F2
|
C:BEF802
|
4.8
|
70.1
|
1.0
|
O2B
|
C:GDP801
|
4.8
|
56.4
|
1.0
|
CD1
|
C:ILE108
|
4.8
|
55.4
|
1.0
|
C
|
C:ILE105
|
4.8
|
45.5
|
1.0
|
N
|
C:HIS107
|
4.8
|
44.3
|
1.0
|
C
|
C:THR84
|
4.9
|
46.4
|
1.0
|
|
Reference:
L.Yan,
Y.Qi,
X.Huang,
C.Yu,
L.Lan,
X.Guo,
Z.Rao,
J.Hu,
Z.Lou.
Structural Basis For Gtp Hydrolysis and Conformational Change of MFN1 in Mediating Membrane Fusion Nat. Struct. Mol. Biol. V. 25 233 2018.
ISSN: ESSN 1545-9985
PubMed: 29483649
DOI: 10.1038/S41594-018-0034-8
Page generated: Mon Aug 12 15:10:14 2024
|