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Zinc in PDB 7v0f: Structure of 6-Carboxy-5,6,7,8-Tetrahydropterin Synthase Paralog QUED2 From Acinetobacter Baumannii

Enzymatic activity of Structure of 6-Carboxy-5,6,7,8-Tetrahydropterin Synthase Paralog QUED2 From Acinetobacter Baumannii

All present enzymatic activity of Structure of 6-Carboxy-5,6,7,8-Tetrahydropterin Synthase Paralog QUED2 From Acinetobacter Baumannii:
4.1.2.50;

Protein crystallography data

The structure of Structure of 6-Carboxy-5,6,7,8-Tetrahydropterin Synthase Paralog QUED2 From Acinetobacter Baumannii, PDB code: 7v0f was solved by M.R.Jordan, G.Gonzalez-Gutierrez, D.P.Giedroc, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.64 / 2.35
Space group I 4
Cell size a, b, c (Å), α, β, γ (°) 84.06, 84.06, 122.42, 90, 90, 90
R / Rfree (%) 23.7 / 27.4

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of 6-Carboxy-5,6,7,8-Tetrahydropterin Synthase Paralog QUED2 From Acinetobacter Baumannii (pdb code 7v0f). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Structure of 6-Carboxy-5,6,7,8-Tetrahydropterin Synthase Paralog QUED2 From Acinetobacter Baumannii, PDB code: 7v0f:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 7v0f

Go back to Zinc Binding Sites List in 7v0f
Zinc binding site 1 out of 4 in the Structure of 6-Carboxy-5,6,7,8-Tetrahydropterin Synthase Paralog QUED2 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 Structure of 6-Carboxy-5,6,7,8-Tetrahydropterin Synthase Paralog QUED2 From Acinetobacter Baumannii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn302

b:41.2
occ:1.00
 O A:HOH416 2.0 44.1 1.0
NE2 A:HIS30 2.2 44.7 1.0
NE2 B:HIS68 2.3 54.3 1.0
ND1 A:HIS28 2.3 50.4 1.0
CE1 A:HIS30 2.8 43.0 1.0
CD2 B:HIS68 2.9 51.9 1.0
CG A:HIS28 2.9 51.6 1.0
CB A:HIS28 3.0 48.4 1.0
CD2 A:HIS30 3.4 42.2 1.0
CE1 A:HIS28 3.4 54.5 1.0
CE1 B:HIS68 3.4 51.2 1.0
CA A:HIS28 3.8 50.2 1.0
ND1 A:HIS30 4.0 43.0 1.0
CG B:HIS68 4.1 51.8 1.0
CD2 A:HIS28 4.2 53.6 1.0
CG A:HIS30 4.3 43.8 1.0
ND1 B:HIS68 4.4 51.7 1.0
NE2 A:HIS28 4.4 57.0 1.0
OE2 A:GLU136 4.6 46.1 1.0
C A:HIS28 4.7 50.7 1.0
N A:HIS28 4.9 53.0 1.0
CD A:GLU136 5.0 43.2 1.0
O A:ILE27 5.0 55.6 1.0

Zinc binding site 2 out of 4 in 7v0f

Go back to Zinc Binding Sites List in 7v0f
Zinc binding site 2 out of 4 in the Structure of 6-Carboxy-5,6,7,8-Tetrahydropterin Synthase Paralog QUED2 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 Structure of 6-Carboxy-5,6,7,8-Tetrahydropterin Synthase Paralog QUED2 From Acinetobacter Baumannii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn303

b:60.7
occ:1.00
 NE2 A:HIS45 2.1 70.1 1.0
NE2 A:HIS188 2.1 75.7 1.0
CE1 A:HIS188 2.8 69.9 1.0
CE1 A:HIS45 3.0 66.9 1.0
CD2 A:HIS45 3.1 70.6 1.0
CD2 A:HIS188 3.3 78.2 1.0
O A:HOH410 3.8 65.6 1.0
ND1 A:HIS188 4.0 72.2 1.0
ND1 A:HIS45 4.1 65.8 1.0
CG A:HIS45 4.2 67.6 1.0
CG A:HIS188 4.3 77.2 1.0

Zinc binding site 3 out of 4 in 7v0f

Go back to Zinc Binding Sites List in 7v0f
Zinc binding site 3 out of 4 in the Structure of 6-Carboxy-5,6,7,8-Tetrahydropterin Synthase Paralog QUED2 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 Structure of 6-Carboxy-5,6,7,8-Tetrahydropterin Synthase Paralog QUED2 From Acinetobacter Baumannii within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn201

b:47.4
occ:1.00
 O B:HOH304 2.0 52.2 1.0
O B:HOH305 2.1 57.3 1.0
NE2 B:HIS30 2.2 51.0 1.0
NE2 A:HIS68 2.2 52.9 1.0
ND1 B:HIS28 2.3 62.4 1.0
CE1 B:HIS30 3.0 46.5 1.0
CD2 A:HIS68 3.1 58.3 1.0
CG B:HIS28 3.2 60.9 1.0
CE1 A:HIS68 3.3 54.5 1.0
CE1 B:HIS28 3.3 69.7 1.0
CB B:HIS28 3.3 56.0 1.0
CD2 B:HIS30 3.4 45.8 1.0
CA B:HIS28 4.0 55.6 1.0
ND1 B:HIS30 4.2 44.5 1.0
CG A:HIS68 4.3 55.5 1.0
OE1 B:GLU136 4.3 49.5 1.0
CD2 B:HIS28 4.4 67.1 1.0
ND1 A:HIS68 4.4 54.5 1.0
NE2 B:HIS28 4.4 73.9 1.0
CG B:HIS30 4.4 46.6 1.0
CD B:GLU136 4.7 47.7 1.0
C B:HIS28 4.9 51.3 1.0
OE2 B:GLU136 4.9 49.9 1.0

Zinc binding site 4 out of 4 in 7v0f

Go back to Zinc Binding Sites List in 7v0f
Zinc binding site 4 out of 4 in the Structure of 6-Carboxy-5,6,7,8-Tetrahydropterin Synthase Paralog QUED2 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 Structure of 6-Carboxy-5,6,7,8-Tetrahydropterin Synthase Paralog QUED2 From Acinetobacter Baumannii within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn202

b:128.3
occ:1.00
 NE2 B:HIS45 2.3 155.8 1.0
CE1 B:HIS45 3.3 151.4 1.0
CD2 B:HIS45 3.3 156.6 1.0
ND1 B:HIS45 4.4 150.9 1.0
CG B:HIS45 4.5 155.0 1.0
OH B:TYR50 4.7 121.9 1.0

Reference:

M.R.Jordan, G.Gonzalez-Gutierrez, J.C.Trinidad, D.P.Giedroc. Metal Retention and Replacement in QUED2 Protect Queuosine-Trna Biosynthesis in Metal-Starved Acinetobacter Baumannii. Proc.Natl.Acad.Sci.Usa V. 119 30119 2022.
ISSN: ESSN 1091-6490
PubMed: 36442121
DOI: 10.1073/PNAS.2213630119
Page generated: Wed Oct 30 12:28:15 2024

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