Zinc in PDB 6v4v: The Crystal Structure of Bona From Acinetobacter Baumannii

Protein crystallography data

The structure of The Crystal Structure of Bona From Acinetobacter Baumannii, PDB code: 6v4v was solved by R.Grinter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.90 / 1.65
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 60.052, 60.052, 99.257, 90, 90, 120
R / Rfree (%) 18.8 / 21.2

Zinc Binding Sites:

The binding sites of Zinc atom in the The Crystal Structure of Bona From Acinetobacter Baumannii (pdb code 6v4v). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the The Crystal Structure of Bona From Acinetobacter Baumannii, PDB code: 6v4v:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 6v4v

Go back to Zinc Binding Sites List in 6v4v
Zinc binding site 1 out of 4 in the The Crystal Structure of Bona From Acinetobacter Baumannii


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Crystal Structure of Bona From Acinetobacter Baumannii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn201

b:39.5
occ:1.00
O A:HOH339 1.9 36.4 1.0
O A:HOH420 2.0 36.1 1.0
O A:HOH415 2.1 35.6 1.0
ND1 A:HIS62 2.2 35.0 1.0
CE1 A:HIS62 3.0 39.2 1.0
CG A:HIS62 3.3 34.7 1.0
CB A:HIS62 3.7 27.8 1.0
O A:HOH441 4.0 57.5 1.0
CA A:HIS62 4.0 27.2 1.0
NE2 A:HIS62 4.2 38.3 1.0
OH A:TYR64 4.2 35.7 1.0
CD2 A:HIS62 4.3 36.3 1.0
CE2 A:TYR64 4.4 28.0 1.0
O A:HOH373 4.4 35.5 1.0
CD2 A:LEU140 4.5 34.7 1.0
CZ A:TYR64 4.7 32.2 1.0
O A:VAL61 4.8 32.9 1.0
N A:HIS62 5.0 24.9 1.0

Zinc binding site 2 out of 4 in 6v4v

Go back to Zinc Binding Sites List in 6v4v
Zinc binding site 2 out of 4 in the The Crystal Structure of Bona From Acinetobacter Baumannii


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The Crystal Structure of Bona From Acinetobacter Baumannii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn202

b:28.0
occ:1.00
O A:HOH383 1.6 36.1 1.0
OE1 A:GLU27 1.9 36.9 1.0
ND1 A:HIS104 2.0 26.2 1.0
O A:HOH386 2.1 30.0 1.0
CD A:GLU27 2.8 36.8 1.0
CE1 A:HIS104 2.9 25.4 1.0
OE2 A:GLU27 3.0 37.4 1.0
CG A:HIS104 3.0 24.4 1.0
CB A:HIS104 3.4 23.8 1.0
O A:HOH317 3.6 34.4 1.0
NE2 A:HIS104 4.0 26.3 1.0
CA A:HIS104 4.1 23.1 1.0
CD2 A:HIS104 4.1 25.2 1.0
CG A:GLU27 4.2 30.2 1.0
O A:VAL103 4.3 28.0 1.0
O A:HOH395 4.4 51.4 0.5
N A:HIS104 5.0 24.0 1.0

Zinc binding site 3 out of 4 in 6v4v

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Zinc binding site 3 out of 4 in the The Crystal Structure of Bona From Acinetobacter Baumannii


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of The Crystal Structure of Bona From Acinetobacter Baumannii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn203

b:51.2
occ:1.00
ND1 A:HIS30 2.1 59.7 1.0
O A:HOH423 2.8 66.3 1.0
CG A:HIS30 3.0 57.1 1.0
CE1 A:HIS30 3.0 59.8 1.0
CB A:HIS30 3.3 49.9 1.0
CA A:HIS30 3.8 42.9 1.0
NE2 A:HIS30 4.1 60.5 1.0
CD2 A:HIS30 4.1 57.6 1.0
N A:HIS30 4.7 36.6 1.0
C A:HIS30 4.9 49.0 1.0

Zinc binding site 4 out of 4 in 6v4v

Go back to Zinc Binding Sites List in 6v4v
Zinc binding site 4 out of 4 in the The Crystal Structure of Bona From Acinetobacter Baumannii


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of The Crystal Structure of Bona From Acinetobacter Baumannii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn204

b:64.4
occ:1.00
O A:HOH304 2.4 39.9 1.0
OE1 A:GLU49 2.6 46.1 1.0
O A:HOH413 2.6 66.7 1.0
CD A:GLU49 3.3 39.9 1.0
OE2 A:GLU49 3.4 33.4 1.0
NZ A:LYS53 4.3 56.4 1.0
OE1 A:GLN46 4.4 36.0 1.0
CG A:GLU49 4.7 28.8 1.0
NE2 A:GLN46 4.7 31.2 1.0
O A:HOH373 4.8 35.5 1.0
CE A:LYS53 4.9 53.7 1.0

Reference:

R.Grinter, F.C.Morris, R.A.Dunstan, P.M.Leung, M.Belousoff, S.D.Gunasinghe, S.Beckham, A.Y.Peleg, C.Greening, J.Li, E.Heinz, T.Lithgow. Bona From Acinetobacter Baumannii Forms A Divisome-Localized Decamer That Supports Outer Envelope Function To Be Published.
Page generated: Mon Jul 12 16:39:24 2021

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