Magnesium in PDB 5fwl: Atomic Cryoem Structure of HSP90-CDC37-CDK4 Complex
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Atomic Cryoem Structure of HSP90-CDC37-CDK4 Complex
(pdb code 5fwl). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the
Atomic Cryoem Structure of HSP90-CDC37-CDK4 Complex, PDB code: 5fwl:
Jump to Magnesium binding site number:
1;
2;
Magnesium binding site 1 out
of 2 in 5fwl
Go back to
Magnesium Binding Sites List in 5fwl
Magnesium binding site 1 out
of 2 in the Atomic Cryoem Structure of HSP90-CDC37-CDK4 Complex
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Atomic Cryoem Structure of HSP90-CDC37-CDK4 Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg1692
b:0.0
occ:1.00
|
OD1
|
A:ASN46
|
1.2
|
0.0
|
1.0
|
O2B
|
A:ATP1691
|
2.0
|
0.0
|
1.0
|
O2A
|
A:ATP1691
|
2.0
|
0.0
|
1.0
|
CG
|
A:ASN46
|
2.3
|
0.0
|
1.0
|
O2G
|
A:ATP1691
|
2.7
|
0.0
|
1.0
|
HD22
|
A:ASN46
|
2.8
|
0.0
|
1.0
|
ND2
|
A:ASN46
|
2.9
|
0.0
|
1.0
|
PA
|
A:ATP1691
|
3.3
|
0.0
|
1.0
|
HA
|
A:ASN46
|
3.3
|
0.0
|
1.0
|
PB
|
A:ATP1691
|
3.4
|
0.0
|
1.0
|
CB
|
A:ASN46
|
3.5
|
0.0
|
1.0
|
O5'
|
A:ATP1691
|
3.5
|
0.0
|
1.0
|
CA
|
A:ASN46
|
3.7
|
0.0
|
1.0
|
H
|
A:ASN46
|
3.8
|
0.0
|
1.0
|
N
|
A:ASN46
|
3.8
|
0.0
|
1.0
|
O
|
A:GLU42
|
3.8
|
0.0
|
1.0
|
HB2
|
A:SER45
|
3.9
|
0.0
|
1.0
|
O3A
|
A:ATP1691
|
3.9
|
0.0
|
1.0
|
HD21
|
A:ASN46
|
3.9
|
0.0
|
1.0
|
PG
|
A:ATP1691
|
4.0
|
0.0
|
1.0
|
O3B
|
A:ATP1691
|
4.1
|
0.0
|
1.0
|
HB3
|
A:ASN46
|
4.1
|
0.0
|
1.0
|
OD2
|
A:ASP49
|
4.1
|
0.0
|
1.0
|
OE1
|
A:GLU42
|
4.2
|
0.0
|
1.0
|
HB2
|
A:ASN46
|
4.3
|
0.0
|
1.0
|
HB3
|
A:SER45
|
4.3
|
0.0
|
1.0
|
C
|
A:SER45
|
4.5
|
0.0
|
1.0
|
O1A
|
A:ATP1691
|
4.5
|
0.0
|
1.0
|
HB3
|
A:GLU42
|
4.5
|
0.0
|
1.0
|
O1B
|
A:ATP1691
|
4.6
|
0.0
|
1.0
|
HA3
|
A:GLY132
|
4.6
|
0.0
|
1.0
|
CB
|
A:SER45
|
4.6
|
0.0
|
1.0
|
C5'
|
A:ATP1691
|
4.6
|
0.0
|
1.0
|
O1G
|
A:ATP1691
|
4.8
|
0.0
|
1.0
|
HA
|
A:GLU42
|
4.8
|
0.0
|
1.0
|
O
|
A:ILE126
|
4.8
|
0.0
|
1.0
|
C
|
A:GLU42
|
4.9
|
0.0
|
1.0
|
O
|
A:SER45
|
5.0
|
0.0
|
1.0
|
H
|
A:PHE133
|
5.0
|
0.0
|
1.0
|
|
Magnesium binding site 2 out
of 2 in 5fwl
Go back to
Magnesium Binding Sites List in 5fwl
Magnesium binding site 2 out
of 2 in the Atomic Cryoem Structure of HSP90-CDC37-CDK4 Complex
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Atomic Cryoem Structure of HSP90-CDC37-CDK4 Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg1693
b:0.0
occ:1.00
|
OD1
|
B:ASN46
|
1.4
|
0.0
|
1.0
|
O2B
|
B:ATP1692
|
2.0
|
0.0
|
1.0
|
O2A
|
B:ATP1692
|
2.0
|
0.0
|
1.0
|
CG
|
B:ASN46
|
2.2
|
0.0
|
1.0
|
O1B
|
B:ATP1692
|
2.4
|
0.0
|
1.0
|
PB
|
B:ATP1692
|
2.5
|
0.0
|
1.0
|
HD22
|
B:ASN46
|
2.6
|
0.0
|
1.0
|
ND2
|
B:ASN46
|
2.8
|
0.0
|
1.0
|
PA
|
B:ATP1692
|
3.3
|
0.0
|
1.0
|
HA
|
B:ASN46
|
3.4
|
0.0
|
1.0
|
O3A
|
B:ATP1692
|
3.4
|
0.0
|
1.0
|
CB
|
B:ASN46
|
3.5
|
0.0
|
1.0
|
O2G
|
B:ATP1692
|
3.5
|
0.0
|
1.0
|
HD21
|
B:ASN46
|
3.6
|
0.0
|
1.0
|
HB3
|
B:ASN46
|
3.7
|
0.0
|
1.0
|
O3B
|
B:ATP1692
|
3.8
|
0.0
|
1.0
|
CA
|
B:ASN46
|
4.0
|
0.0
|
1.0
|
HG
|
B:SER108
|
4.0
|
0.0
|
1.0
|
OD2
|
B:ASP49
|
4.0
|
0.0
|
1.0
|
HA3
|
B:GLY127
|
4.0
|
0.0
|
1.0
|
O5'
|
B:ATP1692
|
4.1
|
0.0
|
1.0
|
HB2
|
B:ASN46
|
4.3
|
0.0
|
1.0
|
HA2
|
B:GLY127
|
4.4
|
0.0
|
1.0
|
PG
|
B:ATP1692
|
4.4
|
0.0
|
1.0
|
HG1
|
B:THR110
|
4.4
|
0.0
|
1.0
|
N
|
B:ASN46
|
4.5
|
0.0
|
1.0
|
O1A
|
B:ATP1692
|
4.5
|
0.0
|
1.0
|
H
|
B:ASN46
|
4.6
|
0.0
|
1.0
|
O
|
B:ILE126
|
4.7
|
0.0
|
1.0
|
O
|
B:GLU42
|
4.7
|
0.0
|
1.0
|
OG1
|
B:THR110
|
4.7
|
0.0
|
1.0
|
CA
|
B:GLY127
|
4.8
|
0.0
|
1.0
|
OG
|
B:SER108
|
4.8
|
0.0
|
1.0
|
HA3
|
B:GLY132
|
4.9
|
0.0
|
1.0
|
|
Reference:
K.A.Verba,
R.Y.Wang,
A.Arakawa,
Y.Liu,
M.Shirouzu,
S.Yokoyama,
D.A.Agard.
Atomic Structure of HSP90-CDC37-CDK4 Reveals That HSP90 Traps and Stabilizes An Unfolded Kinase. Science V. 352 1542 2016.
ISSN: ISSN 0036-8075
PubMed: 27339980
DOI: 10.1126/SCIENCE.AAF5023
Page generated: Sun Sep 29 04:32:31 2024
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