Zinc in PDB 6ivn: Crystal Structure of A Membrane Protein G264A
Protein crystallography data
The structure of Crystal Structure of A Membrane Protein G264A, PDB code: 6ivn
was solved by
A.Kittredge,
F.Fukuda,
Y.Zhang,
T.Yang,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
48.56 /
3.10
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
114.149,
160.939,
160.957,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
21.3 /
26.5
|
Other elements in 6ivn:
The structure of Crystal Structure of A Membrane Protein G264A also contains other interesting chemical elements:
Zinc Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
14;
Binding sites:
The binding sites of Zinc atom in the Crystal Structure of A Membrane Protein G264A
(pdb code 6ivn). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 14 binding sites of Zinc where determined in the
Crystal Structure of A Membrane Protein G264A, PDB code: 6ivn:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Zinc binding site 1 out
of 14 in 6ivn
Go back to
Zinc Binding Sites List in 6ivn
Zinc binding site 1 out
of 14 in the Crystal Structure of A Membrane Protein G264A
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Crystal Structure of A Membrane Protein G264A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn301
b:80.2
occ:1.00
|
OE1
|
A:GLU191
|
1.9
|
84.2
|
1.0
|
O
|
A:HOH401
|
2.0
|
59.9
|
1.0
|
NE2
|
E:HIS194
|
2.0
|
70.4
|
1.0
|
O
|
E:HOH402
|
2.5
|
72.0
|
1.0
|
CD
|
A:GLU191
|
2.8
|
80.8
|
1.0
|
CD2
|
E:HIS194
|
2.9
|
71.4
|
1.0
|
CE1
|
E:HIS194
|
3.1
|
71.9
|
1.0
|
OE2
|
A:GLU191
|
3.1
|
83.0
|
1.0
|
CE
|
A:LYS188
|
4.0
|
91.7
|
1.0
|
CG
|
E:HIS194
|
4.1
|
67.7
|
1.0
|
ND1
|
E:HIS194
|
4.1
|
69.1
|
1.0
|
CG
|
A:GLU191
|
4.2
|
73.8
|
1.0
|
CD
|
A:LYS188
|
4.2
|
86.8
|
1.0
|
CG2
|
A:ILE91
|
4.3
|
60.8
|
1.0
|
CB
|
E:ASP190
|
4.5
|
82.3
|
1.0
|
OG1
|
A:THR95
|
4.8
|
87.0
|
1.0
|
CG
|
E:ASP190
|
4.9
|
93.7
|
1.0
|
NZ
|
A:LYS188
|
4.9
|
97.7
|
1.0
|
OD2
|
E:ASP190
|
4.9
|
0.3
|
1.0
|
O
|
E:ASP190
|
5.0
|
70.4
|
1.0
|
|
Zinc binding site 2 out
of 14 in 6ivn
Go back to
Zinc Binding Sites List in 6ivn
Zinc binding site 2 out
of 14 in the Crystal Structure of A Membrane Protein G264A
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Crystal Structure of A Membrane Protein G264A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn302
b:84.6
occ:1.00
|
CL
|
B:CL304
|
2.0
|
94.1
|
1.0
|
NE2
|
A:HIS194
|
2.1
|
61.0
|
1.0
|
OE1
|
B:GLU191
|
2.4
|
82.7
|
1.0
|
OE2
|
B:GLU191
|
2.5
|
82.7
|
1.0
|
O
|
A:HOH403
|
2.5
|
66.0
|
1.0
|
CD
|
B:GLU191
|
2.7
|
81.0
|
1.0
|
CD2
|
A:HIS194
|
3.0
|
61.1
|
1.0
|
CE1
|
A:HIS194
|
3.1
|
62.1
|
1.0
|
CE
|
B:LYS188
|
4.1
|
84.3
|
1.0
|
CG
|
A:HIS194
|
4.2
|
60.2
|
1.0
|
ND1
|
A:HIS194
|
4.2
|
61.7
|
1.0
|
CG
|
B:GLU191
|
4.2
|
76.7
|
1.0
|
CG2
|
B:ILE91
|
4.4
|
58.6
|
1.0
|
CD
|
B:LYS188
|
4.5
|
84.2
|
1.0
|
CB
|
B:ALA92
|
4.9
|
58.3
|
1.0
|
CA
|
B:ALA92
|
5.0
|
59.0
|
1.0
|
|
Zinc binding site 3 out
of 14 in 6ivn
Go back to
Zinc Binding Sites List in 6ivn
Zinc binding site 3 out
of 14 in the Crystal Structure of A Membrane Protein G264A
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Crystal Structure of A Membrane Protein G264A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn303
b:0.0
occ:1.00
|
ND1
|
A:HIS108
|
2.0
|
0.2
|
1.0
|
O
|
A:HOH402
|
2.1
|
75.9
|
1.0
|
ND1
|
A:HIS111
|
2.2
|
0.4
|
1.0
|
CL
|
A:CL304
|
2.7
|
1.0
|
1.0
|
CE1
|
A:HIS108
|
2.9
|
0.1
|
1.0
|
CG
|
A:HIS108
|
3.0
|
0.2
|
1.0
|
CE1
|
A:HIS111
|
3.1
|
0.9
|
1.0
|
CG
|
A:HIS111
|
3.2
|
0.7
|
1.0
|
CB
|
A:HIS108
|
3.4
|
0.8
|
1.0
|
CB
|
A:HIS111
|
3.5
|
0.5
|
1.0
|
CA
|
A:HIS108
|
3.7
|
0.1
|
1.0
|
NE2
|
A:HIS108
|
4.0
|
0.3
|
1.0
|
CD2
|
A:HIS108
|
4.1
|
0.4
|
1.0
|
CG2
|
A:THR287
|
4.1
|
0.2
|
1.0
|
NE2
|
A:HIS111
|
4.2
|
0.5
|
1.0
|
CD2
|
A:HIS111
|
4.3
|
0.7
|
1.0
|
O
|
A:HIS108
|
4.6
|
0.9
|
1.0
|
N
|
A:HIS108
|
4.6
|
0.9
|
1.0
|
C
|
A:HIS108
|
4.7
|
0.3
|
1.0
|
CB
|
A:THR287
|
4.8
|
0.2
|
1.0
|
O
|
A:GLU107
|
4.9
|
0.1
|
1.0
|
|
Zinc binding site 4 out
of 14 in 6ivn
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Zinc Binding Sites List in 6ivn
Zinc binding site 4 out
of 14 in the Crystal Structure of A Membrane Protein G264A
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Crystal Structure of A Membrane Protein G264A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn301
b:0.3
occ:1.00
|
ND1
|
B:HIS235
|
2.0
|
0.6
|
1.0
|
CL
|
B:CL305
|
2.3
|
0.6
|
1.0
|
CG
|
B:HIS235
|
2.8
|
0.5
|
1.0
|
CB
|
B:HIS235
|
2.9
|
0.9
|
1.0
|
CE1
|
B:HIS235
|
3.2
|
0.5
|
1.0
|
CA
|
B:HIS235
|
3.7
|
0.2
|
1.0
|
CD2
|
B:TYR42
|
4.0
|
0.8
|
1.0
|
CD2
|
B:HIS235
|
4.0
|
0.7
|
1.0
|
NE2
|
B:HIS235
|
4.2
|
0.8
|
1.0
|
CE2
|
B:TYR42
|
4.4
|
0.6
|
1.0
|
C
|
B:HIS235
|
4.7
|
0.9
|
1.0
|
N
|
B:HIS235
|
4.8
|
0.5
|
1.0
|
O
|
B:VAL231
|
4.9
|
87.1
|
1.0
|
N
|
B:TYR236
|
5.0
|
0.6
|
1.0
|
|
Zinc binding site 5 out
of 14 in 6ivn
Go back to
Zinc Binding Sites List in 6ivn
Zinc binding site 5 out
of 14 in the Crystal Structure of A Membrane Protein G264A
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 5 of Crystal Structure of A Membrane Protein G264A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn302
b:79.1
occ:1.00
|
CL
|
D:CL304
|
2.0
|
0.2
|
1.0
|
O
|
B:HOH401
|
2.1
|
70.0
|
1.0
|
NE2
|
B:HIS194
|
2.2
|
64.8
|
1.0
|
OE1
|
D:GLU191
|
2.5
|
86.0
|
1.0
|
OE2
|
D:GLU191
|
2.8
|
90.6
|
1.0
|
CD
|
D:GLU191
|
3.0
|
86.1
|
1.0
|
CD2
|
B:HIS194
|
3.0
|
65.9
|
1.0
|
CE1
|
B:HIS194
|
3.2
|
65.8
|
1.0
|
NZ
|
D:LYS188
|
4.0
|
95.9
|
1.0
|
CG
|
B:HIS194
|
4.2
|
64.8
|
1.0
|
ND1
|
B:HIS194
|
4.2
|
65.7
|
1.0
|
CG2
|
D:ILE91
|
4.4
|
59.7
|
1.0
|
CG
|
D:GLU191
|
4.4
|
81.1
|
1.0
|
CD
|
D:LYS188
|
4.6
|
90.1
|
1.0
|
CB
|
B:ASP190
|
4.7
|
86.5
|
1.0
|
O
|
B:ASP190
|
4.8
|
70.0
|
1.0
|
CE
|
D:LYS188
|
4.8
|
93.8
|
1.0
|
OG1
|
D:THR95
|
4.9
|
85.0
|
1.0
|
|
Zinc binding site 6 out
of 14 in 6ivn
Go back to
Zinc Binding Sites List in 6ivn
Zinc binding site 6 out
of 14 in the Crystal Structure of A Membrane Protein G264A
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 6 of Crystal Structure of A Membrane Protein G264A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn303
b:85.2
occ:1.00
|
ND1
|
B:HIS111
|
2.1
|
73.4
|
1.0
|
CL
|
B:CL306
|
2.2
|
95.2
|
1.0
|
NE2
|
B:HIS290
|
2.3
|
0.6
|
1.0
|
ND1
|
B:HIS108
|
2.4
|
0.6
|
1.0
|
CD2
|
B:HIS290
|
2.9
|
0.2
|
1.0
|
CE1
|
B:HIS111
|
3.0
|
74.0
|
1.0
|
CE1
|
B:HIS108
|
3.1
|
0.1
|
1.0
|
CG
|
B:HIS111
|
3.2
|
75.1
|
1.0
|
CG
|
B:HIS108
|
3.4
|
99.5
|
1.0
|
CE1
|
B:HIS290
|
3.5
|
0.9
|
1.0
|
CB
|
B:HIS111
|
3.5
|
73.7
|
1.0
|
O
|
B:GLY288
|
3.7
|
1.0
|
1.0
|
CA
|
B:HIS108
|
3.8
|
93.9
|
1.0
|
CB
|
B:HIS108
|
3.8
|
97.0
|
1.0
|
NE2
|
B:HIS111
|
4.2
|
75.9
|
1.0
|
CG
|
B:HIS290
|
4.2
|
1.0
|
1.0
|
CD2
|
B:HIS111
|
4.2
|
75.1
|
1.0
|
NE2
|
B:HIS108
|
4.3
|
0.4
|
1.0
|
ND1
|
B:HIS290
|
4.4
|
0.5
|
1.0
|
CD2
|
B:HIS108
|
4.4
|
0.6
|
1.0
|
N
|
B:HIS108
|
4.6
|
91.0
|
1.0
|
O
|
B:HIS108
|
4.7
|
94.4
|
1.0
|
C
|
B:HIS108
|
4.8
|
94.9
|
1.0
|
O
|
B:PRO105
|
4.8
|
93.8
|
1.0
|
CG
|
B:ARG101
|
4.9
|
84.9
|
1.0
|
C
|
B:GLY288
|
4.9
|
0.0
|
1.0
|
NE
|
B:ARG101
|
5.0
|
0.7
|
1.0
|
|
Zinc binding site 7 out
of 14 in 6ivn
Go back to
Zinc Binding Sites List in 6ivn
Zinc binding site 7 out
of 14 in the Crystal Structure of A Membrane Protein G264A
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 7 of Crystal Structure of A Membrane Protein G264A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn301
b:75.7
occ:1.00
|
CL
|
C:CL304
|
2.0
|
91.3
|
1.0
|
NE2
|
D:HIS194
|
2.2
|
62.3
|
1.0
|
OE2
|
C:GLU191
|
2.4
|
79.0
|
1.0
|
OE1
|
C:GLU191
|
2.4
|
69.9
|
1.0
|
CL
|
C:CL305
|
2.4
|
0.6
|
1.0
|
CD
|
C:GLU191
|
2.7
|
73.8
|
1.0
|
CD2
|
D:HIS194
|
3.1
|
63.0
|
1.0
|
CE1
|
D:HIS194
|
3.2
|
64.6
|
1.0
|
NZ
|
C:LYS188
|
3.7
|
78.7
|
1.0
|
CG
|
C:GLU191
|
4.2
|
70.2
|
1.0
|
CG
|
D:HIS194
|
4.2
|
62.7
|
1.0
|
ND1
|
D:HIS194
|
4.3
|
64.2
|
1.0
|
CG2
|
C:ILE91
|
4.5
|
62.1
|
1.0
|
CD
|
C:LYS188
|
4.5
|
72.7
|
1.0
|
CE
|
C:LYS188
|
4.6
|
76.7
|
1.0
|
CB
|
D:ASP190
|
4.9
|
86.5
|
1.0
|
|
Zinc binding site 8 out
of 14 in 6ivn
Go back to
Zinc Binding Sites List in 6ivn
Zinc binding site 8 out
of 14 in the Crystal Structure of A Membrane Protein G264A
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 8 of Crystal Structure of A Membrane Protein G264A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn302
b:81.0
occ:1.00
|
O
|
E:HOH403
|
1.9
|
57.2
|
1.0
|
O
|
C:HOH402
|
2.0
|
85.8
|
1.0
|
NE2
|
C:HIS194
|
2.0
|
57.2
|
1.0
|
OE1
|
E:GLU191
|
2.2
|
78.9
|
1.0
|
OE2
|
E:GLU191
|
2.8
|
81.1
|
1.0
|
CD2
|
C:HIS194
|
2.8
|
58.9
|
1.0
|
CD
|
E:GLU191
|
2.8
|
77.1
|
1.0
|
CE1
|
C:HIS194
|
3.2
|
58.5
|
1.0
|
CG
|
C:HIS194
|
4.0
|
59.0
|
1.0
|
ND1
|
C:HIS194
|
4.2
|
59.2
|
1.0
|
CE
|
E:LYS188
|
4.2
|
83.7
|
1.0
|
CG
|
E:GLU191
|
4.3
|
73.1
|
1.0
|
CD
|
E:LYS188
|
4.3
|
77.7
|
1.0
|
CG2
|
E:ILE91
|
4.4
|
60.8
|
1.0
|
NZ
|
E:LYS188
|
4.6
|
92.0
|
1.0
|
OG1
|
E:THR95
|
4.7
|
70.8
|
1.0
|
O
|
C:ASP190
|
4.8
|
75.1
|
1.0
|
CB
|
C:ASP190
|
4.8
|
85.8
|
1.0
|
|
Zinc binding site 9 out
of 14 in 6ivn
Go back to
Zinc Binding Sites List in 6ivn
Zinc binding site 9 out
of 14 in the Crystal Structure of A Membrane Protein G264A
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 9 of Crystal Structure of A Membrane Protein G264A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn303
b:85.2
occ:1.00
|
ND1
|
C:HIS108
|
2.1
|
80.0
|
1.0
|
ND1
|
C:HIS111
|
2.1
|
83.6
|
1.0
|
CL
|
C:CL306
|
2.2
|
97.9
|
1.0
|
CE1
|
C:HIS111
|
2.9
|
83.4
|
1.0
|
CE1
|
C:HIS108
|
3.0
|
80.7
|
1.0
|
CG
|
C:HIS108
|
3.0
|
80.9
|
1.0
|
CG
|
C:HIS111
|
3.3
|
82.3
|
1.0
|
CB
|
C:HIS108
|
3.4
|
83.3
|
1.0
|
CA
|
C:HIS108
|
3.8
|
87.0
|
1.0
|
CB
|
C:HIS111
|
3.8
|
80.9
|
1.0
|
NE2
|
C:HIS108
|
4.1
|
82.2
|
1.0
|
CD2
|
C:HIS108
|
4.1
|
80.8
|
1.0
|
NE2
|
C:HIS111
|
4.1
|
83.4
|
1.0
|
CD2
|
C:HIS111
|
4.3
|
82.5
|
1.0
|
O
|
C:PRO105
|
4.5
|
0.8
|
1.0
|
NE
|
C:ARG101
|
4.5
|
87.7
|
1.0
|
N
|
C:HIS108
|
4.5
|
87.3
|
1.0
|
NH1
|
C:ARG101
|
4.8
|
94.7
|
1.0
|
C
|
C:HIS108
|
4.9
|
89.5
|
1.0
|
O
|
C:HIS108
|
4.9
|
89.3
|
1.0
|
|
Zinc binding site 10 out
of 14 in 6ivn
Go back to
Zinc Binding Sites List in 6ivn
Zinc binding site 10 out
of 14 in the Crystal Structure of A Membrane Protein G264A
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 10 of Crystal Structure of A Membrane Protein G264A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn307
b:0.3
occ:1.00
|
NE2
|
C:HIS51
|
2.7
|
0.2
|
1.0
|
CE1
|
C:HIS51
|
2.8
|
0.6
|
1.0
|
CG
|
C:GLU46
|
3.5
|
0.4
|
1.0
|
CD
|
C:GLU46
|
3.7
|
0.5
|
1.0
|
OE2
|
C:GLU46
|
3.8
|
0.1
|
1.0
|
CD2
|
C:HIS51
|
4.0
|
0.9
|
1.0
|
CB
|
C:GLU46
|
4.1
|
0.5
|
1.0
|
ND1
|
C:HIS51
|
4.1
|
0.5
|
1.0
|
OE1
|
C:GLU46
|
4.2
|
0.6
|
1.0
|
CA
|
C:GLU46
|
4.7
|
0.6
|
1.0
|
CG
|
C:HIS51
|
4.7
|
0.3
|
1.0
|
|
Reference:
C.Ji,
A.Kittredge,
A.Hopiavuori,
N.Ward,
S.Chen,
Y.Fukuda,
Y.Zhang,
T.Yang.
Dual CA2+-Dependent Gates in Human BESTROPHIN1 Underlie Disease-Causing Mechanisms of Gain-of-Function Mutations. Commun Biol V. 2 240 2019.
ISSN: ESSN 2399-3642
PubMed: 31263784
DOI: 10.1038/S42003-019-0433-3
Page generated: Tue Oct 29 00:23:50 2024
|