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Zinc in PDB 3kwo: Crystal Structure of Putative Bacterioferritin From Campylobacter Jejuni

Protein crystallography data

The structure of Crystal Structure of Putative Bacterioferritin From Campylobacter Jejuni, PDB code: 3kwo was solved by Y.Kim, M.Gu, L.Papazisi, W.Anderson, A.Joachimiak, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.78 / 1.99
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 91.715, 91.715, 202.288, 90.00, 90.00, 120.00
R / Rfree (%) 14.4 / 19.7

Zinc Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 26;

Binding sites:

The binding sites of Zinc atom in the Crystal Structure of Putative Bacterioferritin From Campylobacter Jejuni (pdb code 3kwo). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 26 binding sites of Zinc where determined in the Crystal Structure of Putative Bacterioferritin From Campylobacter Jejuni, PDB code: 3kwo:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Zinc binding site 1 out of 26 in 3kwo

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Zinc binding site 1 out of 26 in the Crystal Structure of Putative Bacterioferritin From Campylobacter Jejuni


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 Putative Bacterioferritin From Campylobacter Jejuni within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn161

b:25.1
occ:1.00
O A:HOH371 2.0 19.5 1.0
O B:HOH198 2.0 23.5 1.0
OXT B:ACY154 2.1 30.6 1.0
NE2 A:HIS37 2.1 17.9 1.0
O B:ACY154 2.5 60.3 1.0
C B:ACY154 2.6 50.6 1.0
CD2 A:HIS37 3.0 16.8 1.0
CE1 A:HIS37 3.2 16.0 1.0
ZN C:ZN164 3.4 18.1 1.0
ZN A:ZN162 3.6 31.4 1.0
CE B:MSE138 3.6 35.0 1.0
OE2 C:GLU56 3.8 16.4 1.0
OE1 C:GLU56 3.8 23.5 1.0
NE2 A:HIS25 3.9 14.8 1.0
CH3 B:ACY154 4.0 54.0 1.0
CE1 A:HIS25 4.0 14.0 1.0
OE1 A:GLU41 4.1 27.8 1.0
CG A:HIS37 4.2 19.3 1.0
CD C:GLU56 4.2 20.9 1.0
ND1 A:HIS37 4.2 14.6 1.0
OE2 A:GLU38 4.5 28.6 1.0
NZ B:LYS134 4.7 58.5 1.0
OD2 C:ASP52 4.8 14.2 1.0
CD A:GLU41 4.8 27.4 1.0
CE B:LYS134 4.9 54.8 1.0
OE2 A:GLU41 4.9 31.5 1.0

Zinc binding site 2 out of 26 in 3kwo

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Zinc binding site 2 out of 26 in the Crystal Structure of Putative Bacterioferritin From Campylobacter Jejuni


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 Putative Bacterioferritin From Campylobacter Jejuni within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn162

b:31.4
occ:1.00
OXT B:ACY154 2.0 30.6 1.0
OE1 A:GLU41 2.1 27.8 1.0
OXT A:ACY153 2.2 38.3 1.0
OE2 A:GLU38 2.2 28.6 1.0
OE1 A:GLU38 2.9 28.9 1.0
CD A:GLU38 2.9 28.9 1.0
CD A:GLU41 3.0 27.4 1.0
C B:ACY154 3.1 50.6 1.0
C A:ACY153 3.1 42.4 1.0
OE2 A:GLU41 3.3 31.5 1.0
O A:ACY153 3.4 48.6 1.0
CH3 B:ACY154 3.5 54.0 1.0
ZN A:ZN161 3.6 25.1 1.0
O A:HOH371 4.0 19.5 1.0
OXT A:ACY152 4.1 54.9 1.0
O B:ACY154 4.2 60.3 1.0
CD2 A:HIS37 4.2 16.8 1.0
CG A:GLU38 4.4 23.1 1.0
CG A:GLU41 4.4 18.8 1.0
CH3 A:ACY153 4.4 38.6 1.0
NE2 A:HIS37 4.5 17.9 1.0
CB A:GLU41 4.6 18.5 1.0
CH3 A:ACY152 4.8 47.1 1.0
CA A:GLU38 4.8 14.0 1.0
C A:ACY152 4.9 51.7 1.0
CE1 A:HIS25 4.9 14.0 1.0

Zinc binding site 3 out of 26 in 3kwo

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Zinc binding site 3 out of 26 in the Crystal Structure of Putative Bacterioferritin From Campylobacter Jejuni


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 Putative Bacterioferritin From Campylobacter Jejuni within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn163

b:51.4
occ:1.00
O A:HOH207 2.3 44.4 1.0
O A:HOH447 2.3 55.3 1.0
OE2 A:GLU45 2.4 35.1 1.0
OE1 A:GLU45 2.6 31.4 1.0
O A:ACY152 2.8 52.1 1.0
CD A:GLU45 2.8 30.3 1.0
OXT A:ACY152 3.1 54.9 1.0
C A:ACY152 3.3 51.7 1.0
OE2 A:GLU41 4.2 31.5 1.0
CG A:GLU45 4.4 22.7 1.0
CG A:GLU41 4.6 18.8 1.0
CD A:GLU41 4.7 27.4 1.0
CH3 A:ACY152 4.8 47.1 1.0

Zinc binding site 4 out of 26 in 3kwo

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Zinc binding site 4 out of 26 in the Crystal Structure of Putative Bacterioferritin From Campylobacter Jejuni


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 Putative Bacterioferritin From Campylobacter Jejuni within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn156

b:19.3
occ:1.00
O A:HOH444 1.8 23.8 1.0
OD2 A:ASP52 1.9 17.8 1.0
NE2 C:HIS25 2.0 16.8 1.0
OE1 A:GLU56 2.0 20.4 1.0
CG A:ASP52 2.7 16.0 1.0
OD1 A:ASP52 2.9 17.4 1.0
CD A:GLU56 2.9 22.2 1.0
CE1 C:HIS25 3.0 13.5 1.0
CD2 C:HIS25 3.0 8.6 1.0
OE2 A:GLU56 3.2 22.3 1.0
ZN C:ZN162 3.3 27.6 1.0
OH C:TYR44 3.6 21.3 1.0
NE2 C:HIS37 3.8 16.6 1.0
CE1 C:HIS37 3.8 15.1 1.0
O A:HOH198 3.9 21.8 1.0
ND1 C:HIS25 4.1 13.3 1.0
CG C:HIS25 4.1 14.4 1.0
CG A:GLU56 4.1 21.5 1.0
CB A:ASP52 4.2 13.4 1.0
O A:HOH495 4.3 48.1 1.0
O C:HOH355 4.4 49.8 1.0
O A:HOH412 4.5 59.8 1.0
NE1 C:TRP26 4.6 13.6 1.0
OE1 C:GLU41 4.7 32.3 1.0
O A:HOH360 4.7 38.5 1.0
CZ C:TYR44 4.7 17.1 1.0
CD1 C:TRP26 4.8 13.4 1.0
CD C:GLU41 4.9 36.2 1.0
OXT C:ACY155 4.9 35.9 1.0
CE2 C:TYR44 4.9 13.8 1.0
ND1 C:HIS37 4.9 12.4 1.0
CD2 C:HIS37 5.0 18.1 1.0

Zinc binding site 5 out of 26 in 3kwo

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Zinc binding site 5 out of 26 in the Crystal Structure of Putative Bacterioferritin From Campylobacter Jejuni


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 Putative Bacterioferritin From Campylobacter Jejuni within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn164

b:32.6
occ:1.00
OE2 A:GLU93 2.1 29.7 1.0
OXT A:ACY159 2.5 70.0 1.0
OXT A:ACY151 2.6 45.4 1.0
OE1 A:GLU93 2.8 33.0 1.0
CD A:GLU93 2.8 30.2 1.0
O A:ACY151 3.0 52.9 1.0
C A:ACY151 3.2 48.6 1.0
C A:ACY159 3.3 73.2 1.0
O A:ACY159 3.4 73.5 1.0
O A:HOH292 3.8 39.6 1.0
CG A:GLU93 4.3 22.2 1.0
CD2 A:LEU89 4.5 22.5 0.4
CH3 A:ACY151 4.7 47.4 1.0
CG A:LEU89 4.7 20.4 0.4
CH3 A:ACY159 4.7 75.1 1.0

Zinc binding site 6 out of 26 in 3kwo

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Zinc binding site 6 out of 26 in the Crystal Structure of Putative Bacterioferritin From Campylobacter Jejuni


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 Putative Bacterioferritin From Campylobacter Jejuni within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn165

b:42.8
occ:1.00
OXT A:ACY155 2.5 40.3 1.0
SG A:CYS68 2.5 29.8 1.0
O A:HOH189 2.6 44.0 1.0
O A:HOH530 2.7 39.9 1.0
C A:ACY155 3.1 44.9 1.0
O A:ACY155 3.1 48.8 1.0
CB A:CYS68 3.5 27.7 1.0
CA A:CYS68 3.7 26.4 1.0
N A:GLN69 3.8 33.5 1.0
C A:CYS68 4.2 29.8 1.0
CG A:GLN69 4.3 40.4 1.0
N A:LYS70 4.5 22.8 1.0
CH3 A:ACY155 4.5 37.0 1.0
CA A:GLN69 4.9 33.0 1.0
CB A:LYS70 5.0 31.1 1.0
O A:HOH291 5.0 41.9 1.0

Zinc binding site 7 out of 26 in 3kwo

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Zinc binding site 7 out of 26 in the Crystal Structure of Putative Bacterioferritin From Campylobacter Jejuni


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 Putative Bacterioferritin From Campylobacter Jejuni within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn167

b:37.8
occ:1.00
OE2 A:GLU111 2.1 29.1 1.0
OE1 A:GLU111 2.6 24.5 1.0
CD A:GLU111 2.7 27.8 1.0
NZ A:LYS115 4.0 39.3 1.0
CG A:GLU111 4.2 23.6 1.0
O A:HOH184 4.2 29.1 1.0
O A:HOH170 4.9 32.1 1.0

Zinc binding site 8 out of 26 in 3kwo

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Zinc binding site 8 out of 26 in the Crystal Structure of Putative Bacterioferritin From Campylobacter Jejuni


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 Putative Bacterioferritin From Campylobacter Jejuni within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn168

b:55.5
occ:1.00
SG A:CYS147 2.3 63.0 1.0
O A:HOH524 2.8 57.4 1.0
CB A:CYS147 3.3 55.6 1.0
N A:CYS147 3.4 47.6 1.0
CA A:CYS147 3.9 56.2 1.0
C A:ALA146 4.4 45.0 1.0
O A:GLY145 4.6 46.2 1.0
CA A:ALA146 4.7 47.5 1.0

Zinc binding site 9 out of 26 in 3kwo

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Zinc binding site 9 out of 26 in the Crystal Structure of Putative Bacterioferritin From Campylobacter Jejuni


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 Putative Bacterioferritin From Campylobacter Jejuni within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn161

b:33.0
occ:1.00
OE1 B:GLU41 2.1 29.0 1.0
OE2 B:GLU38 2.1 29.5 1.0
O B:ACY153 2.2 49.4 1.0
O B:HOH225 2.2 27.0 1.0
C B:ACY153 2.7 54.6 1.0
CD B:GLU38 2.9 25.4 1.0
CD B:GLU41 2.9 29.6 1.0
OXT B:ACY153 2.9 57.6 1.0
OE1 B:GLU38 2.9 26.0 1.0
OE2 B:GLU41 3.0 27.6 1.0
ZN B:ZN162 3.6 27.1 1.0
CH3 B:ACY153 4.0 54.7 1.0
O B:HOH549 4.1 50.0 1.0
CD2 B:HIS37 4.1 17.1 1.0
OXT B:ACY151 4.2 48.5 1.0
NE2 B:HIS37 4.3 19.0 1.0
CG B:GLU38 4.3 15.7 1.0
CG B:GLU41 4.3 22.4 1.0
CB B:GLU41 4.7 17.5 1.0
CH3 B:ACY151 4.8 48.7 1.0
CA B:GLU38 4.8 17.8 1.0
C B:ACY151 5.0 49.3 1.0

Zinc binding site 10 out of 26 in 3kwo

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Zinc binding site 10 out of 26 in the Crystal Structure of Putative Bacterioferritin From Campylobacter Jejuni


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 Putative Bacterioferritin From Campylobacter Jejuni within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn162

b:27.1
occ:1.00
O B:HOH206 1.9 21.6 1.0
O B:HOH225 1.9 27.0 1.0
NE2 B:HIS37 2.0 19.0 1.0
CE1 B:HIS37 2.9 15.0 1.0
CD2 B:HIS37 3.1 17.1 1.0
ZN B:ZN163 3.3 18.8 1.0
ZN B:ZN161 3.6 33.0 1.0
O B:HOH549 3.7 50.0 1.0
CE1 B:HIS25 3.9 13.0 1.0
NE2 B:HIS25 4.0 13.2 1.0
OE1 B:GLU41 4.0 29.0 1.0
ND1 B:HIS37 4.1 16.2 1.0
CG B:HIS37 4.2 15.4 1.0
OE2 B:GLU38 4.5 29.5 1.0
CD B:GLU41 4.6 29.6 1.0
OE2 B:GLU41 4.7 27.6 1.0

Reference:

Y.Kim, M.Gu, L.Papazisi, W.Anderson, A.Joachimiak. Crystal Structure of Putative Bacterioferritin From Campylobacter Jejuni To Be Published.
Page generated: Sat Oct 26 08:14:47 2024

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