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Zinc in PDB 6ggo: Crystal Structure of Salmonella Zinc Metalloprotease Effector Gtga

Protein crystallography data

The structure of Crystal Structure of Salmonella Zinc Metalloprotease Effector Gtga, PDB code: 6ggo was solved by E.Jennings, D.Esposito, K.Rittinger, T.Thurston, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 75.30 / 2.60
Space group I 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 95.783, 40.678, 112.161, 90.00, 94.00, 90.00
R / Rfree (%) 21.8 / 25.5

Other elements in 6ggo:

The structure of Crystal Structure of Salmonella Zinc Metalloprotease Effector Gtga also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Salmonella Zinc Metalloprotease Effector Gtga (pdb code 6ggo). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Salmonella Zinc Metalloprotease Effector Gtga, PDB code: 6ggo:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 6ggo

Go back to Zinc Binding Sites List in 6ggo
Zinc binding site 1 out of 2 in the Crystal Structure of Salmonella Zinc Metalloprotease Effector Gtga


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 Salmonella Zinc Metalloprotease Effector Gtga within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn301

b:85.1
occ:1.00
OD2 B:ASP193 1.9 0.8 1.0
NE2 B:HIS182 2.1 70.0 1.0
NE2 B:HIS186 2.3 82.8 1.0
CG B:ASP193 2.8 0.4 1.0
CL B:CL302 2.9 74.5 1.0
CD2 B:HIS182 2.9 70.4 1.0
HD2 B:HIS182 3.0 78.5 1.0
OD1 B:ASP193 3.0 98.0 1.0
CD2 B:HIS186 3.2 82.8 1.0
CE1 B:HIS182 3.3 67.8 1.0
CE1 B:HIS186 3.3 82.0 1.0
HD2 B:HIS186 3.3 83.9 1.0
HE1 B:TYR224 3.5 97.6 1.0
HE1 B:HIS186 3.5 84.2 1.0
HE1 B:HIS182 3.6 82.6 1.0
O B:HOH415 3.7 68.4 1.0
HE22 B:GLN183 3.8 90.5 1.0
HG11 B:VAL203 4.1 56.1 1.0
CG B:HIS182 4.1 68.4 1.0
CB B:ASP193 4.2 0.5 1.0
OH B:TYR224 4.2 90.8 1.0
CE1 B:TYR224 4.3 84.8 1.0
ND1 B:HIS182 4.3 66.2 1.0
HB2 B:ASP193 4.3 83.6 1.0
CG B:HIS186 4.3 82.3 1.0
ND1 B:HIS186 4.4 82.5 1.0
NE2 B:GLN183 4.4 80.6 1.0
HB3 B:ASP193 4.6 83.6 1.0
CZ B:TYR224 4.7 87.2 1.0
H B:ASP193 4.8 90.3 1.0
HE21 B:GLN183 4.9 90.5 1.0
OE1 B:GLN183 4.9 80.8 1.0
HB B:VAL203 4.9 60.4 1.0
HH B:TYR224 4.9 0.1 1.0
CG1 B:VAL203 5.0 62.9 1.0

Zinc binding site 2 out of 2 in 6ggo

Go back to Zinc Binding Sites List in 6ggo
Zinc binding site 2 out of 2 in the Crystal Structure of Salmonella Zinc Metalloprotease Effector Gtga


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 Salmonella Zinc Metalloprotease Effector Gtga within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:70.9
occ:1.00
OD2 A:ASP193 2.0 76.7 1.0
NE2 A:HIS186 2.2 66.3 1.0
NE2 A:HIS182 2.3 65.7 1.0
CL A:CL302 2.8 60.4 1.0
CG A:ASP193 2.8 77.2 1.0
CD2 A:HIS182 3.0 64.4 1.0
CD2 A:HIS186 3.0 65.4 1.0
OD1 A:ASP193 3.0 76.6 1.0
HD2 A:HIS182 3.0 59.0 1.0
HD2 A:HIS186 3.1 67.4 1.0
CE1 A:HIS186 3.2 66.5 1.0
CE1 A:HIS182 3.4 67.7 1.0
HE1 A:HIS186 3.5 67.7 1.0
HE1 A:TYR224 3.6 98.8 1.0
HE1 A:HIS182 3.6 66.5 1.0
HE22 A:GLN183 3.9 75.9 1.0
HG11 A:VAL203 4.0 49.0 1.0
CG A:HIS186 4.2 64.7 1.0
CB A:ASP193 4.2 79.8 1.0
CG A:HIS182 4.2 64.6 1.0
ND1 A:HIS186 4.3 64.5 1.0
ND1 A:HIS182 4.4 67.5 1.0
HB2 A:ASP193 4.4 71.1 1.0
NE2 A:GLN183 4.5 68.3 1.0
CE1 A:TYR224 4.5 88.6 1.0
H A:ASP193 4.7 81.5 1.0
OH A:TYR224 4.7 87.4 1.0
HB3 A:ASP193 4.7 71.1 1.0
CG1 A:VAL203 4.8 59.2 1.0
HB A:VAL203 4.8 51.7 1.0
OE1 A:GLN183 4.8 66.2 1.0
HG12 A:VAL203 4.9 49.0 1.0
HE21 A:GLN183 4.9 75.9 1.0

Reference:

E.Jennings, D.Esposito, K.Rittinger, T.L.M.Thurston. Structure-Function Analyses of the Bacterial Zinc Metalloprotease Effector Protein Gtga Uncover Key Residues Required For Deactivating Nf-Kappa B. J. Biol. Chem. V. 293 15316 2018.
ISSN: ESSN 1083-351X
PubMed: 30049795
DOI: 10.1074/JBC.RA118.004255
Page generated: Mon Oct 28 21:50:48 2024

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