Zinc in PDB 6ivm: Crystal Structure of A Membrane Protein P143A
Protein crystallography data
The structure of Crystal Structure of A Membrane Protein P143A, PDB code: 6ivm
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)
|
48.72 /
2.95
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
113.965,
158.808,
161.682,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
20.8 /
24.3
|
Other elements in 6ivm:
The structure of Crystal Structure of A Membrane Protein P143A also contains other interesting chemical elements:
Zinc Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
17;
Binding sites:
The binding sites of Zinc atom in the Crystal Structure of A Membrane Protein P143A
(pdb code 6ivm). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 17 binding sites of Zinc where determined in the
Crystal Structure of A Membrane Protein P143A, PDB code: 6ivm:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Zinc binding site 1 out
of 17 in 6ivm
Go back to
Zinc Binding Sites List in 6ivm
Zinc binding site 1 out
of 17 in the Crystal Structure of A Membrane Protein P143A
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 P143A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn301
b:67.3
occ:1.00
|
OE2
|
A:GLU191
|
1.9
|
71.0
|
1.0
|
CL
|
A:CL305
|
2.0
|
71.7
|
1.0
|
NE2
|
E:HIS194
|
2.1
|
55.3
|
1.0
|
O
|
E:HOH408
|
2.4
|
57.0
|
1.0
|
CD
|
A:GLU191
|
2.8
|
68.2
|
1.0
|
CD2
|
E:HIS194
|
3.0
|
53.7
|
1.0
|
CE1
|
E:HIS194
|
3.0
|
56.2
|
1.0
|
OE1
|
A:GLU191
|
3.1
|
70.8
|
1.0
|
ND1
|
E:HIS194
|
4.1
|
56.4
|
1.0
|
CG
|
E:HIS194
|
4.1
|
52.3
|
1.0
|
CG
|
A:GLU191
|
4.2
|
62.5
|
1.0
|
CE
|
A:LYS188
|
4.3
|
67.0
|
1.0
|
CD
|
A:LYS188
|
4.5
|
68.2
|
1.0
|
CG2
|
A:ILE91
|
4.5
|
44.0
|
1.0
|
CB
|
E:ASP190
|
4.8
|
68.3
|
1.0
|
|
Zinc binding site 2 out
of 17 in 6ivm
Go back to
Zinc Binding Sites List in 6ivm
Zinc binding site 2 out
of 17 in the Crystal Structure of A Membrane Protein P143A
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 P143A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn302
b:77.2
occ:1.00
|
CL
|
B:CL305
|
1.9
|
83.0
|
1.0
|
NE2
|
A:HIS194
|
2.2
|
46.9
|
1.0
|
OE1
|
B:GLU191
|
2.3
|
68.8
|
1.0
|
O
|
A:HOH415
|
2.4
|
51.2
|
1.0
|
OE2
|
B:GLU191
|
2.6
|
72.0
|
1.0
|
CD
|
B:GLU191
|
2.8
|
70.9
|
1.0
|
CD2
|
A:HIS194
|
3.2
|
43.8
|
1.0
|
CE1
|
A:HIS194
|
3.2
|
49.4
|
1.0
|
CE
|
B:LYS188
|
4.1
|
59.3
|
1.0
|
CG
|
B:GLU191
|
4.3
|
65.5
|
1.0
|
ND1
|
A:HIS194
|
4.3
|
48.6
|
1.0
|
CG
|
A:HIS194
|
4.4
|
44.5
|
1.0
|
CG2
|
B:ILE91
|
4.6
|
37.9
|
1.0
|
CD
|
B:LYS188
|
4.7
|
54.3
|
1.0
|
CB
|
A:ASP190
|
4.9
|
64.8
|
1.0
|
O
|
A:ASP190
|
5.0
|
54.8
|
1.0
|
|
Zinc binding site 3 out
of 17 in 6ivm
Go back to
Zinc Binding Sites List in 6ivm
Zinc binding site 3 out
of 17 in the Crystal Structure of A Membrane Protein P143A
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 P143A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn303
b:73.5
occ:1.00
|
ND1
|
A:HIS111
|
2.1
|
73.0
|
1.0
|
ND1
|
A:HIS108
|
2.2
|
0.6
|
1.0
|
CL
|
A:CL307
|
2.3
|
96.9
|
1.0
|
CL
|
A:CL306
|
2.5
|
92.5
|
1.0
|
CE1
|
A:HIS111
|
3.1
|
73.3
|
1.0
|
CE1
|
A:HIS108
|
3.1
|
0.3
|
1.0
|
CG
|
A:HIS108
|
3.1
|
93.1
|
1.0
|
CG
|
A:HIS111
|
3.2
|
74.7
|
1.0
|
CB
|
A:HIS108
|
3.5
|
87.0
|
1.0
|
CB
|
A:HIS111
|
3.5
|
73.9
|
1.0
|
CA
|
A:HIS108
|
3.5
|
85.3
|
1.0
|
NE2
|
A:HIS108
|
4.2
|
0.6
|
1.0
|
NE2
|
A:HIS111
|
4.2
|
73.1
|
1.0
|
CD2
|
A:HIS108
|
4.2
|
92.8
|
1.0
|
CD2
|
A:HIS111
|
4.3
|
72.8
|
1.0
|
N
|
A:HIS108
|
4.3
|
91.1
|
1.0
|
O
|
A:HIS108
|
4.6
|
84.9
|
1.0
|
CG2
|
A:THR287
|
4.6
|
70.6
|
1.0
|
C
|
A:HIS108
|
4.6
|
82.6
|
1.0
|
OE1
|
A:GLN289
|
4.8
|
1.0
|
1.0
|
C
|
A:GLU107
|
4.9
|
91.2
|
1.0
|
N
|
A:GLN289
|
4.9
|
0.6
|
1.0
|
O
|
A:PRO105
|
5.0
|
83.2
|
1.0
|
O
|
A:GLU107
|
5.0
|
95.9
|
1.0
|
|
Zinc binding site 4 out
of 17 in 6ivm
Go back to
Zinc Binding Sites List in 6ivm
Zinc binding site 4 out
of 17 in the Crystal Structure of A Membrane Protein P143A
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 P143A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn304
b:79.8
occ:1.00
|
OD2
|
A:ASP269
|
2.0
|
74.0
|
1.0
|
OD2
|
A:ASP261
|
2.3
|
99.1
|
1.0
|
O
|
A:HOH419
|
2.7
|
62.3
|
1.0
|
CG
|
A:ASP269
|
2.9
|
71.3
|
1.0
|
OD1
|
A:ASP269
|
3.0
|
74.3
|
1.0
|
CG
|
A:ASP261
|
3.2
|
90.1
|
1.0
|
CB
|
A:ASP261
|
3.5
|
87.3
|
1.0
|
CB
|
A:ALA266
|
3.5
|
63.6
|
1.0
|
O
|
A:ASP261
|
3.9
|
73.5
|
1.0
|
CA
|
A:GLY264
|
3.9
|
60.6
|
1.0
|
N
|
A:ALA266
|
4.1
|
69.4
|
1.0
|
N
|
A:THR265
|
4.3
|
66.7
|
1.0
|
CB
|
A:ASP269
|
4.3
|
70.1
|
1.0
|
OD1
|
A:ASP261
|
4.4
|
89.3
|
1.0
|
C
|
A:GLY264
|
4.4
|
63.3
|
1.0
|
CA
|
A:ALA266
|
4.4
|
67.8
|
1.0
|
N
|
A:GLY264
|
4.6
|
59.4
|
1.0
|
CA
|
A:ASP261
|
4.7
|
83.4
|
1.0
|
C
|
A:ASP261
|
4.8
|
73.6
|
1.0
|
|
Zinc binding site 5 out
of 17 in 6ivm
Go back to
Zinc Binding Sites List in 6ivm
Zinc binding site 5 out
of 17 in the Crystal Structure of A Membrane Protein P143A
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 P143A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn302
b:0.5
occ:1.00
|
ND1
|
B:HIS235
|
2.4
|
0.6
|
1.0
|
O
|
B:HOH408
|
2.5
|
64.0
|
1.0
|
CG
|
B:HIS235
|
3.1
|
0.6
|
1.0
|
CB
|
B:HIS235
|
3.1
|
0.3
|
1.0
|
CA
|
B:HIS235
|
3.4
|
0.9
|
1.0
|
CE1
|
B:HIS235
|
3.5
|
0.6
|
1.0
|
C
|
B:HIS235
|
4.1
|
0.1
|
1.0
|
CD2
|
B:TYR42
|
4.1
|
94.4
|
1.0
|
O
|
B:HIS235
|
4.3
|
0.5
|
1.0
|
CD2
|
B:HIS235
|
4.3
|
0.2
|
1.0
|
O
|
B:HOH413
|
4.5
|
62.0
|
1.0
|
NE2
|
B:HIS235
|
4.5
|
0.2
|
1.0
|
CE2
|
B:TYR42
|
4.6
|
96.2
|
1.0
|
N
|
B:HIS235
|
4.7
|
0.3
|
1.0
|
N
|
B:TYR236
|
4.8
|
0.0
|
1.0
|
CG
|
B:TYR42
|
4.9
|
92.2
|
1.0
|
CG1
|
B:VAL231
|
5.0
|
85.1
|
1.0
|
|
Zinc binding site 6 out
of 17 in 6ivm
Go back to
Zinc Binding Sites List in 6ivm
Zinc binding site 6 out
of 17 in the Crystal Structure of A Membrane Protein P143A
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 P143A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn303
b:77.4
occ:1.00
|
CL
|
D:CL306
|
2.0
|
81.5
|
1.0
|
NE2
|
B:HIS194
|
2.2
|
52.6
|
1.0
|
O
|
D:HOH408
|
2.2
|
63.1
|
1.0
|
OE2
|
D:GLU191
|
2.5
|
83.7
|
1.0
|
OE1
|
D:GLU191
|
2.5
|
79.2
|
1.0
|
CD
|
D:GLU191
|
2.9
|
77.2
|
1.0
|
CD2
|
B:HIS194
|
3.1
|
50.7
|
1.0
|
CE1
|
B:HIS194
|
3.3
|
53.3
|
1.0
|
NZ
|
D:LYS188
|
3.6
|
75.0
|
1.0
|
CG
|
B:HIS194
|
4.3
|
49.5
|
1.0
|
ND1
|
B:HIS194
|
4.3
|
53.0
|
1.0
|
CG
|
D:GLU191
|
4.4
|
66.2
|
1.0
|
CD
|
D:LYS188
|
4.6
|
63.6
|
1.0
|
CE
|
D:LYS188
|
4.6
|
72.2
|
1.0
|
CG2
|
D:ILE91
|
4.7
|
50.4
|
1.0
|
CB
|
B:ASP190
|
4.7
|
77.3
|
1.0
|
|
Zinc binding site 7 out
of 17 in 6ivm
Go back to
Zinc Binding Sites List in 6ivm
Zinc binding site 7 out
of 17 in the Crystal Structure of A Membrane Protein P143A
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 P143A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn304
b:63.7
occ:1.00
|
ND1
|
B:HIS111
|
2.1
|
57.5
|
1.0
|
NE2
|
B:HIS290
|
2.2
|
90.2
|
1.0
|
ND1
|
B:HIS108
|
2.2
|
78.5
|
1.0
|
O
|
B:ACY306
|
2.4
|
72.9
|
1.0
|
CE1
|
B:HIS111
|
3.0
|
60.5
|
1.0
|
CG
|
B:HIS111
|
3.1
|
56.7
|
1.0
|
CD2
|
B:HIS290
|
3.1
|
91.2
|
1.0
|
CE1
|
B:HIS108
|
3.1
|
80.7
|
1.0
|
CE1
|
B:HIS290
|
3.2
|
92.8
|
1.0
|
C
|
B:ACY306
|
3.3
|
88.4
|
1.0
|
CG
|
B:HIS108
|
3.3
|
74.8
|
1.0
|
OXT
|
B:ACY306
|
3.3
|
89.2
|
1.0
|
CB
|
B:HIS111
|
3.5
|
54.7
|
1.0
|
CB
|
B:HIS108
|
3.6
|
68.4
|
1.0
|
CA
|
B:HIS108
|
3.7
|
65.7
|
1.0
|
NE2
|
B:HIS111
|
4.1
|
61.1
|
1.0
|
CD2
|
B:HIS111
|
4.2
|
58.4
|
1.0
|
O
|
B:GLY288
|
4.3
|
0.9
|
1.0
|
NE2
|
B:HIS108
|
4.3
|
79.2
|
1.0
|
CG
|
B:HIS290
|
4.3
|
95.9
|
1.0
|
ND1
|
B:HIS290
|
4.3
|
94.8
|
1.0
|
CD2
|
B:HIS108
|
4.4
|
79.0
|
1.0
|
N
|
B:HIS108
|
4.5
|
63.0
|
1.0
|
O
|
B:PRO105
|
4.7
|
63.5
|
1.0
|
O
|
B:HIS108
|
4.7
|
67.8
|
1.0
|
CH3
|
B:ACY306
|
4.7
|
79.6
|
1.0
|
C
|
B:HIS108
|
4.7
|
67.5
|
1.0
|
CG
|
B:ARG101
|
4.7
|
62.8
|
1.0
|
NE
|
B:ARG101
|
4.8
|
79.6
|
1.0
|
CA
|
B:HIS111
|
5.0
|
57.2
|
1.0
|
|
Zinc binding site 8 out
of 17 in 6ivm
Go back to
Zinc Binding Sites List in 6ivm
Zinc binding site 8 out
of 17 in the Crystal Structure of A Membrane Protein P143A
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 P143A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn301
b:61.8
occ:1.00
|
CL
|
C:CL304
|
2.0
|
64.0
|
1.0
|
NE2
|
D:HIS194
|
2.1
|
53.6
|
1.0
|
O
|
C:HOH409
|
2.1
|
40.9
|
1.0
|
OE2
|
C:GLU191
|
2.3
|
67.3
|
1.0
|
OE1
|
C:GLU191
|
2.4
|
62.9
|
1.0
|
CD
|
C:GLU191
|
2.7
|
65.6
|
1.0
|
CD2
|
D:HIS194
|
3.0
|
55.0
|
1.0
|
CE1
|
D:HIS194
|
3.2
|
56.8
|
1.0
|
NZ
|
C:LYS188
|
3.7
|
63.9
|
1.0
|
CG
|
D:HIS194
|
4.2
|
54.9
|
1.0
|
CG
|
C:GLU191
|
4.2
|
60.7
|
1.0
|
ND1
|
D:HIS194
|
4.2
|
56.9
|
1.0
|
CG2
|
C:ILE91
|
4.4
|
48.4
|
1.0
|
CD
|
C:LYS188
|
4.8
|
54.4
|
1.0
|
CE
|
C:LYS188
|
4.9
|
57.9
|
1.0
|
CB
|
D:ASP190
|
5.0
|
70.6
|
1.0
|
O
|
D:ASP190
|
5.0
|
55.7
|
1.0
|
|
Zinc binding site 9 out
of 17 in 6ivm
Go back to
Zinc Binding Sites List in 6ivm
Zinc binding site 9 out
of 17 in the Crystal Structure of A Membrane Protein P143A
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 P143A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn302
b:78.1
occ:1.00
|
CL
|
E:CL305
|
2.1
|
98.4
|
1.0
|
NE2
|
C:HIS194
|
2.1
|
45.2
|
1.0
|
OE1
|
E:GLU191
|
2.2
|
64.8
|
1.0
|
O
|
C:HOH407
|
2.7
|
59.6
|
1.0
|
OD1
|
C:ASP190
|
2.8
|
84.2
|
1.0
|
CD
|
E:GLU191
|
2.9
|
65.7
|
1.0
|
OE2
|
E:GLU191
|
2.9
|
70.8
|
1.0
|
CD2
|
C:HIS194
|
3.0
|
47.0
|
1.0
|
CE1
|
C:HIS194
|
3.2
|
45.2
|
1.0
|
CG
|
C:ASP190
|
3.8
|
78.4
|
1.0
|
CE
|
E:LYS188
|
4.0
|
60.6
|
1.0
|
OD2
|
C:ASP190
|
4.0
|
91.1
|
1.0
|
CG
|
C:HIS194
|
4.2
|
45.9
|
1.0
|
CG
|
E:GLU191
|
4.2
|
57.8
|
1.0
|
ND1
|
C:HIS194
|
4.3
|
46.3
|
1.0
|
CD
|
E:LYS188
|
4.7
|
57.6
|
1.0
|
NZ
|
E:LYS188
|
4.8
|
62.4
|
1.0
|
CG2
|
E:ILE91
|
4.8
|
41.7
|
1.0
|
|
Zinc binding site 10 out
of 17 in 6ivm
Go back to
Zinc Binding Sites List in 6ivm
Zinc binding site 10 out
of 17 in the Crystal Structure of A Membrane Protein P143A
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 P143A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn303
b:67.9
occ:1.00
|
ND1
|
C:HIS108
|
1.9
|
62.8
|
1.0
|
ND1
|
C:HIS111
|
2.0
|
66.5
|
1.0
|
CL
|
C:CL305
|
2.3
|
83.6
|
1.0
|
O
|
C:HOH408
|
2.3
|
61.6
|
1.0
|
CE1
|
C:HIS111
|
2.9
|
65.8
|
1.0
|
CE1
|
C:HIS108
|
2.9
|
63.3
|
1.0
|
CG
|
C:HIS108
|
2.9
|
64.4
|
1.0
|
CG
|
C:HIS111
|
3.1
|
65.4
|
1.0
|
CB
|
C:HIS108
|
3.3
|
67.3
|
1.0
|
CB
|
C:HIS111
|
3.5
|
64.4
|
1.0
|
CA
|
C:HIS108
|
3.6
|
72.0
|
1.0
|
NE2
|
C:HIS111
|
4.0
|
66.3
|
1.0
|
NE2
|
C:HIS108
|
4.0
|
66.1
|
1.0
|
CD2
|
C:HIS108
|
4.1
|
63.6
|
1.0
|
CD2
|
C:HIS111
|
4.1
|
64.2
|
1.0
|
NE
|
C:ARG101
|
4.3
|
83.9
|
1.0
|
N
|
C:HIS108
|
4.4
|
75.6
|
1.0
|
O
|
C:PRO105
|
4.6
|
72.8
|
1.0
|
O
|
C:HIS108
|
4.6
|
70.0
|
1.0
|
NH1
|
C:ARG101
|
4.6
|
90.0
|
1.0
|
C
|
C:HIS108
|
4.7
|
72.9
|
1.0
|
CZ
|
C:ARG101
|
4.8
|
82.9
|
1.0
|
CA
|
C:HIS111
|
5.0
|
63.5
|
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 00:22:50 2024
|