Zinc in PDB 6u9v: Cryo Electron Microscopy Structure of the Atp-Gated Rat P2X7 Ion Channel in the Apo, Closed State
Zinc Binding Sites:
The binding sites of Zinc atom in the Cryo Electron Microscopy Structure of the Atp-Gated Rat P2X7 Ion Channel in the Apo, Closed State
(pdb code 6u9v). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the
Cryo Electron Microscopy Structure of the Atp-Gated Rat P2X7 Ion Channel in the Apo, Closed State, PDB code: 6u9v:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
6;
Zinc binding site 1 out
of 6 in 6u9v
Go back to
Zinc Binding Sites List in 6u9v
Zinc binding site 1 out
of 6 in the Cryo Electron Microscopy Structure of the Atp-Gated Rat P2X7 Ion Channel in the Apo, Closed State
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Cryo Electron Microscopy Structure of the Atp-Gated Rat P2X7 Ion Channel in the Apo, Closed State within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn702
b:82.5
occ:1.00
|
SG
|
A:CYS499
|
2.3
|
63.1
|
1.0
|
SG
|
A:CYS506
|
2.3
|
66.5
|
1.0
|
SG
|
A:CYS479
|
2.4
|
70.1
|
1.0
|
SG
|
A:CYS572
|
2.4
|
64.2
|
1.0
|
HB3
|
A:CYS479
|
2.9
|
70.1
|
1.0
|
CB
|
A:CYS479
|
3.0
|
70.1
|
1.0
|
HB2
|
A:CYS479
|
3.1
|
70.1
|
1.0
|
HB3
|
A:CYS499
|
3.1
|
63.1
|
1.0
|
HB3
|
A:CYS572
|
3.1
|
64.2
|
1.0
|
CB
|
A:CYS572
|
3.2
|
64.2
|
1.0
|
HB2
|
A:CYS572
|
3.4
|
64.2
|
1.0
|
CB
|
A:CYS499
|
3.4
|
63.1
|
1.0
|
H
|
A:CYS499
|
3.6
|
63.1
|
1.0
|
CB
|
A:CYS506
|
3.7
|
66.5
|
1.0
|
HB2
|
A:ASN481
|
3.8
|
67.9
|
1.0
|
HA
|
A:CYS506
|
3.8
|
66.5
|
1.0
|
HB2
|
A:CYS506
|
3.9
|
66.5
|
1.0
|
H
|
A:ILE507
|
3.9
|
61.6
|
1.0
|
HB2
|
A:CYS499
|
4.0
|
63.1
|
1.0
|
ZN
|
A:ZN703
|
4.1
|
89.0
|
1.0
|
H
|
A:ASN481
|
4.2
|
67.9
|
1.0
|
N
|
A:CYS499
|
4.3
|
63.1
|
1.0
|
CA
|
A:CYS506
|
4.3
|
66.5
|
1.0
|
HG22
|
A:ILE507
|
4.3
|
61.6
|
1.0
|
CA
|
A:CYS499
|
4.5
|
63.1
|
1.0
|
SG
|
A:CYS498
|
4.5
|
61.9
|
1.0
|
HB3
|
A:CYS506
|
4.5
|
66.5
|
1.0
|
CA
|
A:CYS479
|
4.5
|
70.1
|
1.0
|
H
|
A:CYS572
|
4.5
|
64.2
|
1.0
|
HD22
|
A:ASN481
|
4.6
|
67.9
|
1.0
|
H
|
A:CYS479
|
4.6
|
70.1
|
1.0
|
SG
|
A:CYS482
|
4.6
|
69.8
|
1.0
|
N
|
A:ILE507
|
4.6
|
61.6
|
1.0
|
H
|
A:THR508
|
4.7
|
63.5
|
1.0
|
CA
|
A:CYS572
|
4.7
|
64.2
|
1.0
|
CB
|
A:ASN481
|
4.7
|
67.9
|
1.0
|
H
|
A:GLY480
|
4.8
|
72.0
|
1.0
|
H
|
A:CYS482
|
4.8
|
69.8
|
1.0
|
HB2
|
A:PRO570
|
4.8
|
58.8
|
1.0
|
N
|
A:ASN481
|
4.9
|
67.9
|
1.0
|
C
|
A:CYS506
|
5.0
|
66.5
|
1.0
|
|
Zinc binding site 2 out
of 6 in 6u9v
Go back to
Zinc Binding Sites List in 6u9v
Zinc binding site 2 out
of 6 in the Cryo Electron Microscopy Structure of the Atp-Gated Rat P2X7 Ion Channel in the Apo, Closed State
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Cryo Electron Microscopy Structure of the Atp-Gated Rat P2X7 Ion Channel in the Apo, Closed State within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn703
b:89.0
occ:1.00
|
HB2
|
A:CYS477
|
1.5
|
69.6
|
1.0
|
CB
|
A:CYS477
|
2.1
|
69.6
|
1.0
|
SG
|
A:CYS482
|
2.3
|
69.8
|
1.0
|
SG
|
A:CYS477
|
2.3
|
69.6
|
1.0
|
SG
|
A:CYS479
|
2.3
|
70.1
|
1.0
|
SG
|
A:CYS498
|
2.4
|
61.9
|
1.0
|
HB3
|
A:CYS477
|
2.7
|
69.6
|
1.0
|
H
|
A:CYS479
|
2.8
|
70.1
|
1.0
|
HB2
|
A:CYS482
|
3.0
|
69.8
|
1.0
|
CB
|
A:CYS482
|
3.3
|
69.8
|
1.0
|
CA
|
A:CYS477
|
3.3
|
69.6
|
1.0
|
H
|
A:GLN478
|
3.5
|
68.5
|
1.0
|
N
|
A:CYS479
|
3.5
|
70.1
|
1.0
|
HA
|
A:CYS477
|
3.5
|
69.6
|
1.0
|
CB
|
A:CYS479
|
3.6
|
70.1
|
1.0
|
H
|
A:CYS482
|
3.7
|
69.8
|
1.0
|
CB
|
A:CYS498
|
3.7
|
61.9
|
1.0
|
HB2
|
A:CYS498
|
3.7
|
61.9
|
1.0
|
N
|
A:GLN478
|
3.7
|
68.5
|
1.0
|
HA
|
A:CYS498
|
3.7
|
61.9
|
1.0
|
C
|
A:CYS477
|
3.8
|
69.6
|
1.0
|
HB3
|
A:CYS479
|
3.9
|
70.1
|
1.0
|
CA
|
A:CYS479
|
3.9
|
70.1
|
1.0
|
H
|
A:CYS499
|
3.9
|
63.1
|
1.0
|
HB3
|
A:CYS482
|
4.0
|
69.8
|
1.0
|
ZN
|
A:ZN702
|
4.1
|
82.5
|
1.0
|
C
|
A:CYS479
|
4.1
|
70.1
|
1.0
|
O
|
A:CYS479
|
4.2
|
70.1
|
1.0
|
N
|
A:CYS482
|
4.2
|
69.8
|
1.0
|
CA
|
A:CYS498
|
4.3
|
61.9
|
1.0
|
CA
|
A:CYS482
|
4.3
|
69.8
|
1.0
|
HB2
|
A:CYS479
|
4.4
|
70.1
|
1.0
|
HB3
|
A:CYS498
|
4.5
|
61.9
|
1.0
|
C
|
A:GLN478
|
4.5
|
68.5
|
1.0
|
HZ3
|
A:TRP476
|
4.5
|
67.7
|
1.0
|
HB3
|
A:CYS572
|
4.5
|
64.2
|
1.0
|
N
|
A:CYS477
|
4.6
|
69.6
|
1.0
|
HA
|
A:CYS482
|
4.6
|
69.8
|
1.0
|
O
|
A:CYS477
|
4.6
|
69.6
|
1.0
|
H
|
A:CYS477
|
4.7
|
69.6
|
1.0
|
N
|
A:CYS499
|
4.7
|
63.1
|
1.0
|
CA
|
A:GLN478
|
4.7
|
68.5
|
1.0
|
N
|
A:GLY480
|
4.8
|
72.0
|
1.0
|
SG
|
A:CYS572
|
4.8
|
64.2
|
1.0
|
H
|
A:ASN481
|
4.8
|
67.9
|
1.0
|
HA
|
A:CYS479
|
4.9
|
70.1
|
1.0
|
SG
|
A:CYS499
|
4.9
|
63.1
|
1.0
|
|
Zinc binding site 3 out
of 6 in 6u9v
Go back to
Zinc Binding Sites List in 6u9v
Zinc binding site 3 out
of 6 in the Cryo Electron Microscopy Structure of the Atp-Gated Rat P2X7 Ion Channel in the Apo, Closed State
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Cryo Electron Microscopy Structure of the Atp-Gated Rat P2X7 Ion Channel in the Apo, Closed State within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn702
b:78.9
occ:1.00
|
SG
|
B:CYS499
|
2.3
|
62.4
|
1.0
|
SG
|
B:CYS506
|
2.3
|
64.9
|
1.0
|
SG
|
B:CYS572
|
2.3
|
62.9
|
1.0
|
SG
|
B:CYS479
|
2.4
|
69.4
|
1.0
|
HB3
|
B:CYS479
|
2.8
|
69.4
|
1.0
|
CB
|
B:CYS479
|
2.9
|
69.4
|
1.0
|
HB2
|
B:CYS479
|
3.0
|
69.4
|
1.0
|
HB3
|
B:CYS572
|
3.2
|
62.9
|
1.0
|
HB3
|
B:CYS499
|
3.2
|
62.4
|
1.0
|
CB
|
B:CYS572
|
3.3
|
62.9
|
1.0
|
CB
|
B:CYS499
|
3.4
|
62.4
|
1.0
|
HB2
|
B:CYS572
|
3.5
|
62.9
|
1.0
|
H
|
B:CYS499
|
3.6
|
62.4
|
1.0
|
CB
|
B:CYS506
|
3.8
|
64.9
|
1.0
|
HA
|
B:CYS506
|
3.8
|
64.9
|
1.0
|
HB2
|
B:ASN481
|
3.9
|
66.5
|
1.0
|
HB2
|
B:CYS506
|
3.9
|
64.9
|
1.0
|
H
|
B:ILE507
|
3.9
|
60.5
|
1.0
|
HB2
|
B:CYS499
|
4.1
|
62.4
|
1.0
|
ZN
|
B:ZN703
|
4.2
|
89.7
|
1.0
|
H
|
B:ASN481
|
4.2
|
66.5
|
1.0
|
HG22
|
B:ILE507
|
4.2
|
60.5
|
1.0
|
N
|
B:CYS499
|
4.3
|
62.4
|
1.0
|
CA
|
B:CYS506
|
4.3
|
64.9
|
1.0
|
CA
|
B:CYS479
|
4.4
|
69.4
|
1.0
|
H
|
B:CYS572
|
4.5
|
62.9
|
1.0
|
HB3
|
B:CYS506
|
4.5
|
64.9
|
1.0
|
CA
|
B:CYS499
|
4.5
|
62.4
|
1.0
|
H
|
B:CYS479
|
4.5
|
69.4
|
1.0
|
SG
|
B:CYS498
|
4.6
|
62.5
|
1.0
|
N
|
B:ILE507
|
4.6
|
60.5
|
1.0
|
HD22
|
B:ASN481
|
4.6
|
66.5
|
1.0
|
H
|
B:THR508
|
4.7
|
62.5
|
1.0
|
HB2
|
B:PRO570
|
4.7
|
57.9
|
1.0
|
CA
|
B:CYS572
|
4.7
|
62.9
|
1.0
|
H
|
B:GLY480
|
4.7
|
70.4
|
1.0
|
CB
|
B:ASN481
|
4.8
|
66.5
|
1.0
|
H
|
B:CYS482
|
4.8
|
69.1
|
1.0
|
SG
|
B:CYS482
|
4.8
|
69.1
|
1.0
|
N
|
B:ASN481
|
4.9
|
66.5
|
1.0
|
HA
|
B:CYS479
|
5.0
|
69.4
|
1.0
|
N
|
B:CYS479
|
5.0
|
69.4
|
1.0
|
C
|
B:CYS506
|
5.0
|
64.9
|
1.0
|
|
Zinc binding site 4 out
of 6 in 6u9v
Go back to
Zinc Binding Sites List in 6u9v
Zinc binding site 4 out
of 6 in the Cryo Electron Microscopy Structure of the Atp-Gated Rat P2X7 Ion Channel in the Apo, Closed State
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Cryo Electron Microscopy Structure of the Atp-Gated Rat P2X7 Ion Channel in the Apo, Closed State within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn703
b:89.7
occ:1.00
|
HB2
|
B:CYS477
|
1.5
|
69.9
|
1.0
|
CB
|
B:CYS477
|
2.1
|
69.9
|
1.0
|
SG
|
B:CYS482
|
2.3
|
69.1
|
1.0
|
SG
|
B:CYS477
|
2.3
|
69.9
|
1.0
|
SG
|
B:CYS479
|
2.3
|
69.4
|
1.0
|
SG
|
B:CYS498
|
2.3
|
62.5
|
1.0
|
H
|
B:CYS479
|
2.6
|
69.4
|
1.0
|
HB3
|
B:CYS477
|
2.7
|
69.9
|
1.0
|
HB2
|
B:CYS482
|
2.9
|
69.1
|
1.0
|
H
|
B:GLN478
|
3.0
|
68.2
|
1.0
|
CB
|
B:CYS482
|
3.2
|
69.1
|
1.0
|
N
|
B:CYS479
|
3.3
|
69.4
|
1.0
|
CA
|
B:CYS477
|
3.4
|
69.9
|
1.0
|
HA
|
B:CYS477
|
3.5
|
69.9
|
1.0
|
N
|
B:GLN478
|
3.5
|
68.2
|
1.0
|
CB
|
B:CYS479
|
3.6
|
69.4
|
1.0
|
CB
|
B:CYS498
|
3.7
|
62.5
|
1.0
|
HB2
|
B:CYS498
|
3.8
|
62.5
|
1.0
|
H
|
B:CYS482
|
3.8
|
69.1
|
1.0
|
HA
|
B:CYS498
|
3.8
|
62.5
|
1.0
|
C
|
B:CYS477
|
3.8
|
69.9
|
1.0
|
HB3
|
B:CYS479
|
3.9
|
69.4
|
1.0
|
HB3
|
B:CYS482
|
3.9
|
69.1
|
1.0
|
CA
|
B:CYS479
|
3.9
|
69.4
|
1.0
|
H
|
B:CYS499
|
4.0
|
62.4
|
1.0
|
C
|
B:CYS479
|
4.1
|
69.4
|
1.0
|
ZN
|
B:ZN702
|
4.2
|
78.9
|
1.0
|
O
|
B:CYS479
|
4.2
|
69.4
|
1.0
|
CA
|
B:CYS482
|
4.3
|
69.1
|
1.0
|
N
|
B:CYS482
|
4.3
|
69.1
|
1.0
|
CA
|
B:CYS498
|
4.3
|
62.5
|
1.0
|
C
|
B:GLN478
|
4.4
|
68.2
|
1.0
|
HZ3
|
B:TRP476
|
4.4
|
67.7
|
1.0
|
HB2
|
B:CYS479
|
4.4
|
69.4
|
1.0
|
HA
|
B:CYS482
|
4.5
|
69.1
|
1.0
|
HB3
|
B:CYS498
|
4.5
|
62.5
|
1.0
|
CA
|
B:GLN478
|
4.5
|
68.2
|
1.0
|
N
|
B:CYS477
|
4.6
|
69.9
|
1.0
|
H
|
B:CYS477
|
4.6
|
69.9
|
1.0
|
N
|
B:CYS499
|
4.8
|
62.4
|
1.0
|
HA
|
B:CYS479
|
4.8
|
69.4
|
1.0
|
HB3
|
B:CYS572
|
4.9
|
62.9
|
1.0
|
CZ3
|
B:TRP476
|
4.9
|
67.7
|
1.0
|
N
|
B:GLY480
|
4.9
|
70.4
|
1.0
|
O
|
B:CYS477
|
4.9
|
69.9
|
1.0
|
SG
|
B:CYS499
|
4.9
|
62.4
|
1.0
|
SG
|
B:CYS572
|
5.0
|
62.9
|
1.0
|
|
Zinc binding site 5 out
of 6 in 6u9v
Go back to
Zinc Binding Sites List in 6u9v
Zinc binding site 5 out
of 6 in the Cryo Electron Microscopy Structure of the Atp-Gated Rat P2X7 Ion Channel in the Apo, Closed State
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 5 of Cryo Electron Microscopy Structure of the Atp-Gated Rat P2X7 Ion Channel in the Apo, Closed State within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn702
b:81.9
occ:1.00
|
SG
|
C:CYS499
|
2.3
|
62.5
|
1.0
|
SG
|
C:CYS506
|
2.3
|
65.8
|
1.0
|
SG
|
C:CYS572
|
2.3
|
63.5
|
1.0
|
SG
|
C:CYS479
|
2.4
|
69.4
|
1.0
|
HB3
|
C:CYS479
|
2.9
|
69.4
|
1.0
|
CB
|
C:CYS479
|
3.1
|
69.4
|
1.0
|
HB2
|
C:CYS479
|
3.1
|
69.4
|
1.0
|
HB3
|
C:CYS499
|
3.2
|
62.5
|
1.0
|
HB3
|
C:CYS572
|
3.2
|
63.5
|
1.0
|
CB
|
C:CYS572
|
3.3
|
63.5
|
1.0
|
CB
|
C:CYS499
|
3.4
|
62.5
|
1.0
|
HB2
|
C:CYS572
|
3.4
|
63.5
|
1.0
|
H
|
C:CYS499
|
3.6
|
62.5
|
1.0
|
CB
|
C:CYS506
|
3.7
|
65.8
|
1.0
|
HB2
|
C:CYS506
|
3.8
|
65.8
|
1.0
|
HA
|
C:CYS506
|
3.8
|
65.8
|
1.0
|
HB2
|
C:ASN481
|
3.8
|
66.7
|
1.0
|
H
|
C:ILE507
|
3.9
|
61.1
|
1.0
|
HB2
|
C:CYS499
|
4.0
|
62.5
|
1.0
|
ZN
|
C:ZN703
|
4.1
|
90.2
|
1.0
|
H
|
C:ASN481
|
4.2
|
66.7
|
1.0
|
HG22
|
C:ILE507
|
4.2
|
61.1
|
1.0
|
CA
|
C:CYS506
|
4.3
|
65.8
|
1.0
|
N
|
C:CYS499
|
4.3
|
62.5
|
1.0
|
HB3
|
C:CYS506
|
4.5
|
65.8
|
1.0
|
CA
|
C:CYS499
|
4.5
|
62.5
|
1.0
|
H
|
C:CYS572
|
4.5
|
63.5
|
1.0
|
CA
|
C:CYS479
|
4.5
|
69.4
|
1.0
|
N
|
C:ILE507
|
4.6
|
61.1
|
1.0
|
SG
|
C:CYS498
|
4.6
|
61.6
|
1.0
|
H
|
C:CYS479
|
4.6
|
69.4
|
1.0
|
HD22
|
C:ASN481
|
4.6
|
66.7
|
1.0
|
H
|
C:THR508
|
4.6
|
62.9
|
1.0
|
HB2
|
C:PRO570
|
4.7
|
58.1
|
1.0
|
SG
|
C:CYS482
|
4.7
|
68.8
|
1.0
|
CA
|
C:CYS572
|
4.7
|
63.5
|
1.0
|
CB
|
C:ASN481
|
4.8
|
66.7
|
1.0
|
H
|
C:GLY480
|
4.8
|
71.1
|
1.0
|
H
|
C:CYS482
|
4.8
|
68.8
|
1.0
|
N
|
C:ASN481
|
5.0
|
66.7
|
1.0
|
C
|
C:CYS506
|
5.0
|
65.8
|
1.0
|
|
Zinc binding site 6 out
of 6 in 6u9v
Go back to
Zinc Binding Sites List in 6u9v
Zinc binding site 6 out
of 6 in the Cryo Electron Microscopy Structure of the Atp-Gated Rat P2X7 Ion Channel in the Apo, Closed State
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 6 of Cryo Electron Microscopy Structure of the Atp-Gated Rat P2X7 Ion Channel in the Apo, Closed State within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn703
b:90.2
occ:1.00
|
HB2
|
C:CYS477
|
1.8
|
68.8
|
1.0
|
SG
|
C:CYS482
|
2.3
|
68.8
|
1.0
|
SG
|
C:CYS477
|
2.3
|
68.8
|
1.0
|
SG
|
C:CYS498
|
2.3
|
61.6
|
1.0
|
SG
|
C:CYS479
|
2.3
|
69.4
|
1.0
|
CB
|
C:CYS477
|
2.4
|
68.8
|
1.0
|
H
|
C:CYS479
|
2.6
|
69.4
|
1.0
|
HB2
|
C:CYS482
|
2.9
|
68.8
|
1.0
|
HB3
|
C:CYS477
|
3.0
|
68.8
|
1.0
|
H
|
C:GLN478
|
3.1
|
68.0
|
1.0
|
CB
|
C:CYS482
|
3.2
|
68.8
|
1.0
|
N
|
C:CYS479
|
3.4
|
69.4
|
1.0
|
CB
|
C:CYS479
|
3.6
|
69.4
|
1.0
|
CA
|
C:CYS477
|
3.6
|
68.8
|
1.0
|
N
|
C:GLN478
|
3.6
|
68.0
|
1.0
|
CB
|
C:CYS498
|
3.7
|
61.6
|
1.0
|
H
|
C:CYS482
|
3.7
|
68.8
|
1.0
|
HA
|
C:CYS498
|
3.8
|
61.6
|
1.0
|
HB2
|
C:CYS498
|
3.8
|
61.6
|
1.0
|
HA
|
C:CYS477
|
3.8
|
68.8
|
1.0
|
HB3
|
C:CYS479
|
3.8
|
69.4
|
1.0
|
CA
|
C:CYS479
|
3.8
|
69.4
|
1.0
|
HB3
|
C:CYS482
|
3.9
|
68.8
|
1.0
|
H
|
C:CYS499
|
3.9
|
62.5
|
1.0
|
C
|
C:CYS477
|
4.0
|
68.8
|
1.0
|
ZN
|
C:ZN702
|
4.1
|
81.9
|
1.0
|
C
|
C:CYS479
|
4.1
|
69.4
|
1.0
|
O
|
C:CYS479
|
4.1
|
69.4
|
1.0
|
N
|
C:CYS482
|
4.2
|
68.8
|
1.0
|
CA
|
C:CYS482
|
4.3
|
68.8
|
1.0
|
CA
|
C:CYS498
|
4.3
|
61.6
|
1.0
|
HB2
|
C:CYS479
|
4.4
|
69.4
|
1.0
|
C
|
C:GLN478
|
4.4
|
68.0
|
1.0
|
HB3
|
C:CYS498
|
4.5
|
61.6
|
1.0
|
HA
|
C:CYS482
|
4.5
|
68.8
|
1.0
|
HZ3
|
C:TRP476
|
4.6
|
67.0
|
1.0
|
CA
|
C:GLN478
|
4.6
|
68.0
|
1.0
|
HB3
|
C:CYS572
|
4.6
|
63.5
|
1.0
|
N
|
C:CYS499
|
4.7
|
62.5
|
1.0
|
HA
|
C:CYS479
|
4.8
|
69.4
|
1.0
|
N
|
C:GLY480
|
4.8
|
71.1
|
1.0
|
SG
|
C:CYS572
|
4.8
|
63.5
|
1.0
|
SG
|
C:CYS499
|
4.8
|
62.5
|
1.0
|
N
|
C:CYS477
|
4.8
|
68.8
|
1.0
|
H
|
C:CYS477
|
4.9
|
68.8
|
1.0
|
H
|
C:ASN481
|
4.9
|
66.7
|
1.0
|
|
Reference:
A.E.Mccarthy,
C.Yoshioka,
S.E.Mansoor.
Full-Length P2X7STRUCTURES Reveal How Palmitoylation Prevents Channel Desensitization. Cell V. 179 659 2019.
ISSN: ISSN 1097-4172
PubMed: 31587896
DOI: 10.1016/J.CELL.2019.09.017
Page generated: Tue Oct 29 08:29:39 2024
|