Zinc in PDB 6iv0: Crystal Structure of A Bacterial Bestrophin Homolog From Klebsiella Pneumoniae with A Mutation I180A

The structure of Crystal Structure of A Bacterial Bestrophin Homolog From Klebsiella Pneumoniae with A Mutation I180A, PDB code: 6iv0 was solved by S.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	65.38 / 2.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	113.573, 159.905, 161.261, 90.00, 90.00, 90.00
R / Rfree (%)	20.1 / 23.8

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>>> Page 1 <<< Page 2, Binding sites: 11 - 15;

Binding sites:

The binding sites of Zinc atom in the Crystal Structure of A Bacterial Bestrophin Homolog From Klebsiella Pneumoniae with A Mutation I180A (pdb code 6iv0). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 15 binding sites of Zinc where determined in the Crystal Structure of A Bacterial Bestrophin Homolog From Klebsiella Pneumoniae with A Mutation I180A, PDB code: 6iv0:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Zinc binding site 1 out of 15 in the Crystal Structure of A Bacterial Bestrophin Homolog From Klebsiella Pneumoniae with A Mutation I180A


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 Bacterial Bestrophin Homolog From Klebsiella Pneumoniae with A Mutation I180A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:74.1 occ:1.00 OE2 A:GLU191 2.0 82.3 1.0 NE2 E:HIS194 2.1 61.4 1.0 O A:HOH402 2.2 57.4 1.0 O A:HOH401 2.3 51.6 1.0 CD A:GLU191 2.8 75.2 1.0 OE1 A:GLU191 2.9 68.7 1.0 CE1 E:HIS194 2.9 61.3 1.0 CD2 E:HIS194 3.1 59.3 1.0 ND1 E:HIS194 4.0 56.5 1.0 CG E:HIS194 4.1 48.7 1.0 CE A:LYS188 4.2 70.6 1.0 CD A:LYS188 4.2 69.3 1.0 CG A:GLU191 4.2 65.3 1.0 CG2 A:ILE91 4.5 48.3 1.0 CB E:ASP190 4.6 56.3 1.0 O E:ASP190 4.9 52.0 1.0 OG1 A:THR95 5.0 58.9 1.0

Zinc binding site 2 out of 15 in the Crystal Structure of A Bacterial Bestrophin Homolog From Klebsiella Pneumoniae with A Mutation I180A


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 Bacterial Bestrophin Homolog From Klebsiella Pneumoniae with A Mutation I180A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:76.7 occ:1.00 O B:HOH403 2.2 63.1 1.0 NE2 A:HIS194 2.3 45.6 1.0 OE1 B:GLU191 2.4 60.9 1.0 OE2 B:GLU191 2.7 61.4 1.0 O A:HOH405 2.7 51.8 1.0 CD B:GLU191 2.9 64.8 1.0 CD2 A:HIS194 3.1 44.9 1.0 CE1 A:HIS194 3.3 50.7 1.0 CE B:LYS188 4.1 65.0 1.0 CG A:HIS194 4.3 45.3 1.0 CD B:LYS188 4.3 58.3 1.0 ND1 A:HIS194 4.4 48.7 1.0 CG B:GLU191 4.4 54.3 1.0 CG2 B:ILE91 4.6 37.0 1.0 CB A:ASP190 4.8 61.0 1.0 O A:ASP190 4.9 49.2 1.0

Zinc binding site 3 out of 15 in the Crystal Structure of A Bacterial Bestrophin Homolog From Klebsiella Pneumoniae with A Mutation I180A


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 Bacterial Bestrophin Homolog From Klebsiella Pneumoniae with A Mutation I180A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn303 b:81.9 occ:1.00 ND1 A:HIS108 2.0 90.5 1.0 O A:HOH404 2.1 72.8 1.0 ND1 A:HIS111 2.1 76.1 1.0 O A:HOH406 2.7 73.7 1.0 CE1 A:HIS108 2.9 88.2 1.0 CE1 A:HIS111 3.0 77.5 1.0 CG A:HIS108 3.1 86.7 1.0 CG A:HIS111 3.1 81.7 1.0 CB A:HIS111 3.5 75.6 1.0 CB A:HIS108 3.5 82.1 1.0 CA A:HIS108 3.8 80.5 1.0 NE2 A:HIS108 4.0 86.6 1.0 CD2 A:HIS108 4.1 81.8 1.0 NE2 A:HIS111 4.2 74.4 1.0 CD2 A:HIS111 4.2 75.9 1.0 CG2 A:THR287 4.4 80.8 1.0 N A:HIS108 4.6 80.5 1.0 O A:GLU107 4.6 85.0 1.0 O A:HIS108 4.8 77.3 1.0 CB A:THR287 4.8 86.5 1.0 C A:HIS108 4.8 78.4 1.0 C A:GLU107 5.0 82.2 1.0 CA A:HIS111 5.0 70.3 1.0

Zinc binding site 4 out of 15 in the Crystal Structure of A Bacterial Bestrophin Homolog From Klebsiella Pneumoniae with A Mutation I180A


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 Bacterial Bestrophin Homolog From Klebsiella Pneumoniae with A Mutation I180A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn304 b:81.0 occ:1.00 OD2 A:ASP269 2.2 73.5 1.0 OD2 A:ASP261 2.5 91.0 1.0 O A:HOH407 2.8 70.8 1.0 CG A:ASP269 3.1 72.2 1.0 CG A:ASP261 3.4 87.5 1.0 OD1 A:ASP269 3.4 76.4 1.0 CB A:ASP261 3.5 76.3 1.0 CB A:ALA266 3.5 61.4 1.0 CA A:GLY264 3.6 68.5 1.0 O A:ASP261 3.9 75.0 1.0 N A:ALA266 4.0 70.0 1.0 N A:THR265 4.1 71.3 1.0 C A:GLY264 4.3 70.1 1.0 CA A:ALA266 4.4 68.4 1.0 N A:GLY264 4.5 68.5 1.0 CB A:ASP269 4.5 70.0 1.0 OD1 A:ASP261 4.6 93.8 1.0 CA A:ASP261 4.7 78.7 1.0 C A:ASP261 4.7 75.5 1.0

Zinc binding site 5 out of 15 in the Crystal Structure of A Bacterial Bestrophin Homolog From Klebsiella Pneumoniae with A Mutation I180A


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 Bacterial Bestrophin Homolog From Klebsiella Pneumoniae with A Mutation I180A within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn301 b:0.1 occ:0.99 O B:HOH401 2.2 30.0 1.0 ND1 B:HIS235 2.5 0.2 1.0 CG B:HIS235 3.4 0.6 1.0 CE1 B:HIS235 3.4 0.6 1.0 CB B:HIS235 3.6 0.8 1.0 CA B:HIS235 3.7 0.9 1.0 CD2 B:TYR42 3.8 0.3 1.0 CE2 B:TYR42 4.1 0.9 1.0 NE2 B:HIS235 4.5 0.8 1.0 CD2 B:HIS235 4.5 0.0 1.0 C B:HIS235 4.6 0.8 1.0 NE2 B:GLN43 4.7 0.6 1.0 CG B:TYR42 4.8 98.7 1.0 N B:HIS235 4.8 0.9 1.0 CG2 B:VAL231 4.9 99.6 1.0

Zinc binding site 6 out of 15 in the Crystal Structure of A Bacterial Bestrophin Homolog From Klebsiella Pneumoniae with A Mutation I180A


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 Bacterial Bestrophin Homolog From Klebsiella Pneumoniae with A Mutation I180A within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn302 b:73.2 occ:1.00 ND1 B:HIS108 2.1 82.6 1.0 ND1 B:HIS111 2.2 64.7 1.0 O B:HOH402 2.5 65.7 1.0 NE2 B:HIS290 2.5 78.9 1.0 CE1 B:HIS108 2.9 76.7 1.0 CE1 B:HIS111 3.1 69.0 1.0 CG B:HIS108 3.2 75.2 1.0 CG B:HIS111 3.2 64.7 1.0 CE1 B:HIS290 3.4 85.5 1.0 NH2 B:ARG101 3.4 0.6 1.0 CD2 B:HIS290 3.5 89.6 1.0 CB B:HIS111 3.5 60.4 1.0 CB B:HIS108 3.6 68.3 1.0 CA B:HIS108 3.8 66.4 1.0 NE2 B:HIS108 4.1 68.3 1.0 O B:GLY288 4.2 97.1 1.0 CD2 B:HIS108 4.2 65.3 1.0 NE2 B:HIS111 4.3 64.9 1.0 CD2 B:HIS111 4.3 65.5 1.0 ND1 B:HIS290 4.4 92.9 1.0 CG B:HIS290 4.5 92.7 1.0 CZ B:ARG101 4.6 94.3 1.0 N B:HIS108 4.6 65.7 1.0 O B:PRO105 4.6 72.9 1.0 O B:HIS108 4.7 79.3 1.0 C B:HIS108 4.8 74.7 1.0 CG B:ARG101 4.8 65.2 1.0

Zinc binding site 7 out of 15 in the Crystal Structure of A Bacterial Bestrophin Homolog From Klebsiella Pneumoniae with A Mutation I180A


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 Bacterial Bestrophin Homolog From Klebsiella Pneumoniae with A Mutation I180A within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn301 b:69.8 occ:1.00 O C:HOH402 2.0 56.0 1.0 NE2 D:HIS194 2.0 62.3 1.0 O C:HOH404 2.3 61.5 1.0 OE1 C:GLU191 2.4 65.2 1.0 OE2 C:GLU191 2.4 71.4 1.0 CD C:GLU191 2.7 72.8 1.0 CD2 D:HIS194 3.0 57.7 1.0 CE1 D:HIS194 3.1 63.5 1.0 NZ C:LYS188 3.5 67.6 1.0 CG D:HIS194 4.1 54.9 1.0 ND1 D:HIS194 4.1 60.6 1.0 CG C:GLU191 4.3 61.7 1.0 CG2 C:ILE91 4.5 53.2 1.0 CD C:LYS188 4.7 65.1 1.0 CE C:LYS188 4.7 61.7 1.0 CB D:ASP190 4.8 62.2 1.0 O D:ASP190 4.9 55.5 1.0

Zinc binding site 8 out of 15 in the Crystal Structure of A Bacterial Bestrophin Homolog From Klebsiella Pneumoniae with A Mutation I180A


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 Bacterial Bestrophin Homolog From Klebsiella Pneumoniae with A Mutation I180A within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn302 b:76.5 occ:1.00 NE2 C:HIS194 2.2 53.0 1.0 OE1 E:GLU191 2.3 64.9 1.0 O C:HOH401 2.4 59.4 1.0 O C:HOH406 2.4 30.0 1.0 OE2 E:GLU191 2.7 70.5 1.0 CD E:GLU191 2.8 64.2 1.0 CD2 C:HIS194 3.0 53.4 1.0 NZ E:LYS188 3.3 72.7 1.0 OD1 C:ASP190 3.3 79.2 1.0 CE1 C:HIS194 3.4 52.3 1.0 OD2 C:ASP190 3.5 83.5 1.0 CG C:ASP190 3.7 75.2 1.0 CG C:HIS194 4.3 48.1 1.0 CG E:GLU191 4.4 49.0 1.0 ND1 C:HIS194 4.4 47.5 1.0 CE E:LYS188 4.5 67.7 1.0 CD E:LYS188 4.6 63.3 1.0 CG2 E:ILE91 4.8 46.8 1.0 O C:ASP190 4.9 54.4 1.0

Zinc binding site 9 out of 15 in the Crystal Structure of A Bacterial Bestrophin Homolog From Klebsiella Pneumoniae with A Mutation I180A


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 Bacterial Bestrophin Homolog From Klebsiella Pneumoniae with A Mutation I180A within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn303 b:75.5 occ:1.00 ND1 C:HIS108 2.0 80.0 1.0 ND1 C:HIS111 2.2 77.5 1.0 O C:HOH405 2.3 68.8 1.0 O C:HOH403 2.4 77.2 1.0 CE1 C:HIS108 2.8 79.1 1.0 CG C:HIS108 3.0 76.5 1.0 CE1 C:HIS111 3.1 75.7 1.0 CG C:HIS111 3.2 74.7 1.0 CB C:HIS111 3.5 72.1 1.0 CB C:HIS108 3.5 79.0 1.0 CA C:HIS108 3.6 79.5 1.0 NE2 C:HIS108 4.0 79.7 1.0 CD2 C:HIS108 4.1 81.5 1.0 NE C:ARG101 4.1 88.9 1.0 NE2 C:HIS111 4.3 76.3 1.0 CD2 C:HIS111 4.3 73.3 1.0 N C:HIS108 4.4 82.9 1.0 NH1 C:ARG101 4.6 92.4 1.0 O C:PRO105 4.7 80.3 1.0 C C:HIS108 4.7 78.6 1.0 CZ C:ARG101 4.7 89.3 1.0 O C:HIS108 4.7 72.6 1.0 CD C:ARG101 4.9 77.0 1.0 CG C:ARG101 5.0 67.9 1.0 CA C:HIS111 5.0 67.9 1.0

Zinc binding site 10 out of 15 in the Crystal Structure of A Bacterial Bestrophin Homolog From Klebsiella Pneumoniae with A Mutation I180A


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 Bacterial Bestrophin Homolog From Klebsiella Pneumoniae with A Mutation I180A within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn301 b:76.7 occ:1.00 NE2 B:HIS194 2.2 60.2 1.0 O D:HOH401 2.3 71.5 1.0 O B:HOH404 2.3 66.8 1.0 OE2 D:GLU191 2.5 79.4 1.0 OE1 D:GLU191 2.7 68.3 1.0 CD D:GLU191 3.0 73.0 1.0 CD2 B:HIS194 3.1 60.4 1.0 CE1 B:HIS194 3.3 62.0 1.0 NZ D:LYS188 3.3 81.7 1.0 CG B:HIS194 4.3 60.5 1.0 ND1 B:HIS194 4.4 60.6 1.0 CD D:LYS188 4.4 68.1 1.0 CE D:LYS188 4.4 78.0 1.0 CG D:GLU191 4.5 60.1 1.0 CB B:ASP190 4.5 64.9 1.0 CG2 D:ILE91 4.6 53.4 1.0 O B:ASP190 4.8 59.2 1.0

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