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Chlorine in PDB 6ivo: Crystal Structure of A Membrane Protein P208A

Protein crystallography data

The structure of Crystal Structure of A Membrane Protein P208A, PDB code: 6ivo 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) 48.76 / 2.45
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 114.009, 160.062, 161.843, 90.00, 90.00, 90.00
R / Rfree (%) 20.2 / 23.8

Other elements in 6ivo:

The structure of Crystal Structure of A Membrane Protein P208A also contains other interesting chemical elements:

Zinc (Zn) 18 atoms
Sodium (Na) 1 atom

Chlorine Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 12;

Binding sites:

The binding sites of Chlorine atom in the Crystal Structure of A Membrane Protein P208A (pdb code 6ivo). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 12 binding sites of Chlorine where determined in the Crystal Structure of A Membrane Protein P208A, PDB code: 6ivo:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Chlorine binding site 1 out of 12 in 6ivo

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Chlorine binding site 1 out of 12 in the Crystal Structure of A Membrane Protein P208A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of A Membrane Protein P208A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl308

b:63.2
occ:1.00
 ZN A:ZN301 2.2 58.0 1.0
OE2 A:GLU191 3.2 69.1 1.0
OD2 E:ASP190 3.3 82.1 1.0
CG2 A:THR95 3.3 37.2 1.0
NE2 E:HIS194 3.4 41.0 1.0
OG1 A:THR95 3.4 46.1 1.0
CD A:LYS188 3.5 50.1 1.0
CE A:LYS188 3.6 61.9 1.0
CG E:ASP190 3.7 62.4 1.0
O A:HOH428 3.8 47.2 1.0
CD2 E:HIS194 3.8 32.3 1.0
CB A:THR95 3.9 36.7 1.0
CG2 A:ILE91 4.1 39.5 1.0
CD A:GLU191 4.1 65.3 1.0
CA A:ALA92 4.2 35.7 1.0
OE1 A:GLU191 4.2 61.8 1.0
CB E:ASP190 4.3 48.8 1.0
NZ A:LYS188 4.3 80.6 1.0
O A:ILE91 4.4 37.7 1.0
OD1 E:ASP190 4.4 67.2 1.0
CE1 E:HIS194 4.5 41.4 1.0
O E:ASP190 4.6 41.0 1.0
CA E:ASP190 4.6 43.2 1.0
C A:ILE91 4.6 38.3 1.0
N A:ALA92 4.6 36.6 1.0
CB A:ALA92 4.8 35.9 1.0
CG A:LYS188 4.8 44.0 1.0

Chlorine binding site 2 out of 12 in 6ivo

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Chlorine binding site 2 out of 12 in the Crystal Structure of A Membrane Protein P208A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of A Membrane Protein P208A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl309

b:64.0
occ:1.00
 ZN A:ZN303 2.1 57.8 1.0
ND1 A:HIS108 3.3 64.2 1.0
CL A:CL310 3.4 68.3 1.0
CE1 A:HIS108 3.5 61.7 1.0
ND1 A:HIS111 3.5 46.0 1.0
O A:HOH405 3.5 76.7 1.0
NE A:ARG101 3.6 69.4 1.0
CZ A:ARG101 3.7 70.0 1.0
CD A:ARG101 3.9 64.8 1.0
CE1 A:HIS111 4.0 48.7 1.0
CA A:THR287 4.0 61.0 1.0
NH2 A:ARG101 4.1 67.1 1.0
CG A:ARG101 4.1 57.7 1.0
NH1 A:ARG101 4.1 71.0 1.0
CG2 A:THR287 4.3 56.0 1.0
CB A:THR287 4.3 59.7 1.0
C A:THR287 4.4 64.1 1.0
O A:MET286 4.4 52.5 1.0
O A:THR287 4.4 65.6 1.0
CG A:HIS111 4.6 49.2 1.0
CG A:HIS108 4.6 61.0 1.0
NE2 A:HIS108 4.8 66.7 1.0

Chlorine binding site 3 out of 12 in 6ivo

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Chlorine binding site 3 out of 12 in the Crystal Structure of A Membrane Protein P208A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of A Membrane Protein P208A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl310

b:68.3
occ:1.00
 ZN A:ZN303 2.1 57.8 1.0
ND1 A:HIS108 3.4 64.2 1.0
CL A:CL309 3.4 64.0 1.0
CB A:HIS111 3.5 47.3 1.0
ND1 A:HIS111 3.6 46.0 1.0
CB A:HIS108 3.7 60.9 1.0
O A:THR287 3.7 65.6 1.0
CB A:THR287 3.8 59.7 1.0
O A:HIS108 3.8 61.5 1.0
CG A:HIS108 4.0 61.0 1.0
CA A:HIS108 4.0 59.7 1.0
CG A:HIS111 4.1 49.2 1.0
CG A:ARG112 4.1 71.6 1.0
CG2 A:THR287 4.2 56.0 1.0
NH1 A:ARG112 4.2 90.1 1.0
C A:HIS108 4.4 59.5 1.0
CA A:THR287 4.5 61.0 1.0
C A:THR287 4.5 64.1 1.0
CE1 A:HIS108 4.5 61.7 1.0
N A:ARG112 4.7 56.8 1.0
CD A:ARG112 4.8 87.2 1.0
OG1 A:THR287 4.8 55.9 1.0
OE1 A:GLN289 4.8 0.5 1.0
CA A:HIS111 4.9 49.5 1.0
CE1 A:HIS111 4.9 48.7 1.0

Chlorine binding site 4 out of 12 in 6ivo

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Chlorine binding site 4 out of 12 in the Crystal Structure of A Membrane Protein P208A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of A Membrane Protein P208A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl311

b:70.6
occ:1.00
 ND1 A:HIS235 3.4 94.6 1.0
CE1 A:HIS235 3.5 0.5 1.0
CG A:HIS235 4.0 92.4 1.0
NE2 E:HIS51 4.1 62.0 1.0
NE2 A:HIS235 4.2 0.9 1.0
O A:GLY232 4.4 78.8 1.0
CD2 A:HIS235 4.5 98.8 1.0
CD2 E:HIS51 4.5 60.0 1.0
CE2 A:TYR42 4.5 97.2 1.0
CB A:HIS235 4.6 78.9 1.0

Chlorine binding site 5 out of 12 in 6ivo

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Chlorine binding site 5 out of 12 in the Crystal Structure of A Membrane Protein P208A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Crystal Structure of A Membrane Protein P208A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl308

b:75.2
occ:1.00
 ZN A:ZN302 2.2 59.4 1.0
OG1 B:THR95 3.3 44.5 1.0
CG2 B:THR95 3.4 39.1 1.0
CD B:LYS188 3.4 54.5 1.0
CE B:LYS188 3.4 62.3 1.0
OE1 B:GLU191 3.5 61.0 1.0
NE2 A:HIS194 3.5 41.0 1.0
CB A:ASP190 3.8 56.1 1.0
CB B:THR95 3.9 41.6 1.0
CD2 A:HIS194 3.9 37.3 1.0
CG A:ASP190 3.9 71.9 1.0
O A:HOH434 4.0 50.8 1.0
CG2 B:ILE91 4.1 35.0 1.0
OD1 A:ASP190 4.3 89.2 1.0
NZ B:LYS188 4.3 74.8 1.0
OD2 A:ASP190 4.3 82.5 1.0
CA B:ALA92 4.3 36.2 1.0
CD B:GLU191 4.4 64.1 1.0
CA A:ASP190 4.4 47.2 1.0
O B:ILE91 4.4 36.0 1.0
OE2 B:GLU191 4.5 75.0 1.0
O A:ASP190 4.6 45.0 1.0
CE1 A:HIS194 4.6 40.1 1.0
C B:ILE91 4.8 35.4 1.0
N B:ALA92 4.8 34.6 1.0
CG B:LYS188 4.9 46.4 1.0
CB B:ALA92 4.9 34.2 1.0
C A:ASP190 4.9 43.1 1.0

Chlorine binding site 6 out of 12 in 6ivo

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Chlorine binding site 6 out of 12 in the Crystal Structure of A Membrane Protein P208A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of Crystal Structure of A Membrane Protein P208A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl309

b:78.0
occ:1.00
 ZN B:ZN302 2.2 61.3 1.0
OE1 D:GLU191 3.2 68.8 1.0
CG2 D:THR95 3.3 44.2 1.0
OD2 B:ASP190 3.3 85.5 1.0
NE2 B:HIS194 3.4 43.1 1.0
CD D:LYS188 3.5 58.7 1.0
OG1 D:THR95 3.5 53.2 1.0
CE D:LYS188 3.6 62.4 1.0
CG B:ASP190 3.6 77.7 1.0
O B:HOH427 3.6 52.8 1.0
NZ D:LYS188 3.7 84.4 1.0
CD2 B:HIS194 3.8 35.6 1.0
CG2 D:ILE91 4.0 37.6 1.0
CB D:THR95 4.0 45.4 1.0
OD1 B:ASP190 4.1 88.6 1.0
CB B:ASP190 4.2 62.4 1.0
CD D:GLU191 4.2 68.5 1.0
CA D:ALA92 4.3 41.6 1.0
O D:ILE91 4.4 43.6 1.0
CE1 B:HIS194 4.5 39.5 1.0
CA B:ASP190 4.5 51.3 1.0
O B:ASP190 4.5 45.9 1.0
OE2 D:GLU191 4.5 72.8 1.0
N D:ALA92 4.6 41.5 1.0
C D:ILE91 4.6 39.5 1.0
CG D:LYS188 4.9 54.3 1.0
C B:ASP190 4.9 47.4 1.0
CG B:HIS194 5.0 39.5 1.0
CB D:ALA92 5.0 39.3 1.0

Chlorine binding site 7 out of 12 in 6ivo

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Chlorine binding site 7 out of 12 in the Crystal Structure of A Membrane Protein P208A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 7 of Crystal Structure of A Membrane Protein P208A within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl306

b:57.2
occ:1.00
 ZN C:ZN301 2.2 52.4 1.0
NZ C:LYS188 3.3 73.1 1.0
CG2 C:THR95 3.3 39.5 1.0
NE2 D:HIS194 3.4 39.5 1.0
OG1 C:THR95 3.4 54.6 1.0
O C:HOH429 3.5 47.3 1.0
OE1 C:GLU191 3.6 55.9 1.0
CD2 D:HIS194 3.7 39.1 1.0
CD C:LYS188 3.9 58.7 1.0
CE C:LYS188 3.9 62.9 1.0
CB C:THR95 3.9 44.2 1.0
CG2 C:ILE91 3.9 39.9 1.0
CB D:ASP190 4.0 52.7 1.0
CG D:ASP190 4.1 65.2 1.0
OE2 C:GLU191 4.2 59.3 1.0
CA C:ALA92 4.2 39.8 1.0
CD C:GLU191 4.3 55.7 1.0
OD1 D:ASP190 4.4 65.9 1.0
O C:ILE91 4.4 41.7 1.0
O D:ASP190 4.5 46.0 1.0
CA D:ASP190 4.5 47.5 1.0
N C:ALA92 4.5 42.1 1.0
CE1 D:HIS194 4.6 40.9 1.0
C C:ILE91 4.6 40.8 1.0
OD2 D:ASP190 4.6 75.1 1.0
CB C:ALA92 4.8 36.9 1.0
C D:ASP190 4.9 46.4 1.0
CG D:HIS194 5.0 41.0 1.0

Chlorine binding site 8 out of 12 in 6ivo

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Chlorine binding site 8 out of 12 in the Crystal Structure of A Membrane Protein P208A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 8 of Crystal Structure of A Membrane Protein P208A within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl307

b:67.0
occ:1.00
 ZN C:ZN303 2.2 53.4 1.0
NE C:ARG101 3.2 75.1 1.0
CA C:THR287 3.3 61.5 1.0
ND1 C:HIS108 3.3 42.8 1.0
ND1 C:HIS111 3.4 53.1 1.0
CE1 C:HIS108 3.5 43.5 1.0
CB C:THR287 3.5 58.4 1.0
CD C:ARG101 3.6 66.6 1.0
CG2 C:THR287 3.7 58.0 1.0
CZ C:ARG101 3.7 75.3 1.0
C C:THR287 3.8 66.2 1.0
O C:THR287 3.8 67.2 1.0
O C:MET286 4.0 53.8 1.0
CB C:HIS111 4.0 50.6 1.0
CG C:HIS111 4.0 53.0 1.0
CG C:ARG101 4.1 56.6 1.0
NH1 C:ARG101 4.2 77.4 1.0
NH2 C:ARG101 4.3 75.4 1.0
CE1 C:HIS111 4.3 53.5 1.0
N C:THR287 4.5 58.0 1.0
C C:MET286 4.7 52.2 1.0
CG C:HIS108 4.7 44.3 1.0
NE2 C:HIS108 4.8 49.2 1.0
O C:HOH420 4.8 64.0 1.0
N C:GLY288 4.8 68.1 1.0
OG1 C:THR287 4.9 53.2 1.0

Chlorine binding site 9 out of 12 in 6ivo

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Chlorine binding site 9 out of 12 in the Crystal Structure of A Membrane Protein P208A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 9 of Crystal Structure of A Membrane Protein P208A within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl307

b:78.0
occ:1.00
 ZN D:ZN301 2.2 71.0 1.0
NE D:ARG101 3.2 71.3 1.0
CL D:CL308 3.4 87.8 1.0
CD D:ARG101 3.5 68.1 1.0
ND1 D:HIS108 3.6 82.5 1.0
ND1 D:HIS111 3.6 56.5 1.0
CZ D:ARG101 3.6 71.7 1.0
CA D:THR287 3.8 82.6 1.0
CE1 D:HIS108 3.8 83.6 1.0
N D:GLY288 3.9 0.0 1.0
CG D:ARG101 4.0 55.9 1.0
NH1 D:ARG101 4.0 79.7 1.0
CG2 D:THR287 4.0 76.9 1.0
CB D:THR287 4.1 83.2 1.0
C D:THR287 4.2 91.1 1.0
CE1 D:HIS111 4.2 56.5 1.0
NH2 D:ARG101 4.2 64.3 1.0
O D:GLY288 4.2 0.5 1.0
O D:MET286 4.4 68.5 1.0
CG D:HIS111 4.7 54.6 1.0
CG D:HIS108 4.8 78.0 1.0
C D:GLY288 4.8 0.4 1.0
CA D:GLY288 4.9 0.1 1.0
CB D:HIS111 5.0 51.3 1.0

Chlorine binding site 10 out of 12 in 6ivo

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Chlorine binding site 10 out of 12 in the Crystal Structure of A Membrane Protein P208A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 10 of Crystal Structure of A Membrane Protein P208A within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl308

b:87.8
occ:1.00
 ZN D:ZN301 2.3 71.0 1.0
CL D:CL307 3.4 78.0 1.0
N D:GLY288 3.4 0.0 1.0
ND1 D:HIS108 3.6 82.5 1.0
CB D:HIS111 3.6 51.3 1.0
NH1 D:ARG112 3.7 0.6 1.0
CB D:THR287 3.7 83.2 1.0
CB D:HIS108 3.7 63.0 1.0
O D:HIS108 3.8 58.8 1.0
ND1 D:HIS111 3.9 56.5 1.0
CG2 D:THR287 3.9 76.9 1.0
CA D:HIS108 3.9 62.8 1.0
CG D:ARG112 4.0 93.3 1.0
CA D:GLY288 4.0 0.1 1.0
CG D:HIS108 4.1 78.0 1.0
CG D:HIS111 4.2 54.6 1.0
C D:HIS108 4.3 60.3 1.0
C D:THR287 4.4 91.1 1.0
CA D:THR287 4.4 82.6 1.0
C D:GLY288 4.6 0.4 1.0
CD D:ARG112 4.6 0.6 1.0
CE1 D:HIS108 4.7 83.6 1.0
OG1 D:THR287 4.7 75.6 1.0
N D:ARG112 4.8 64.0 1.0
CZ D:ARG112 4.8 0.4 1.0
CA D:HIS111 4.9 52.2 1.0
O D:GLY288 4.9 0.5 1.0
C D:HIS111 5.0 60.5 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: Sat Jul 12 15:51:46 2025

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