Zinc in PDB 7yp8: Neisseria Gonorrhoeae Leucyl-Trna Synthetase in Complex with Leucyl- Sulfamoyl 3-Deazaadenosine

Enzymatic activity of Neisseria Gonorrhoeae Leucyl-Trna Synthetase in Complex with Leucyl- Sulfamoyl 3-Deazaadenosine

All present enzymatic activity of Neisseria Gonorrhoeae Leucyl-Trna Synthetase in Complex with Leucyl- Sulfamoyl 3-Deazaadenosine:
6.1.1.4;

Protein crystallography data

The structure of Neisseria Gonorrhoeae Leucyl-Trna Synthetase in Complex with Leucyl- Sulfamoyl 3-Deazaadenosine, PDB code: 7yp8 was solved by L.Pang, S.De Graef, S.V.Strelkov, S.D.Weeks, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 56.21 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 48.794, 82.979, 229.25, 90, 90, 90
R / Rfree (%) 17.9 / 23.1

Other elements in 7yp8:

The structure of Neisseria Gonorrhoeae Leucyl-Trna Synthetase in Complex with Leucyl- Sulfamoyl 3-Deazaadenosine also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Neisseria Gonorrhoeae Leucyl-Trna Synthetase in Complex with Leucyl- Sulfamoyl 3-Deazaadenosine (pdb code 7yp8). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Neisseria Gonorrhoeae Leucyl-Trna Synthetase in Complex with Leucyl- Sulfamoyl 3-Deazaadenosine, PDB code: 7yp8:

Zinc binding site 1 out of 1 in 7yp8

Go back to Zinc Binding Sites List in 7yp8
Zinc binding site 1 out of 1 in the Neisseria Gonorrhoeae Leucyl-Trna Synthetase in Complex with Leucyl- Sulfamoyl 3-Deazaadenosine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Neisseria Gonorrhoeae Leucyl-Trna Synthetase in Complex with Leucyl- Sulfamoyl 3-Deazaadenosine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1003

b:49.2
occ:1.00
 SG A:CYS452 2.3 58.5 1.0
SG A:CYS490 2.3 46.6 1.0
SG A:CYS493 2.4 52.2 1.0
SG A:CYS449 2.4 49.0 1.0
CB A:CYS490 3.1 43.5 1.0
CB A:CYS493 3.2 41.7 1.0
CB A:CYS452 3.3 58.7 1.0
CB A:CYS449 3.3 53.6 1.0
N A:CYS493 3.7 43.2 1.0
N A:CYS452 3.8 53.4 1.0
CA A:CYS493 4.0 48.8 1.0
CA A:CYS452 4.2 53.7 1.0
O A:HOH1233 4.4 45.6 1.0
CB A:LYS451 4.5 60.0 1.0
CB A:CYS492 4.5 58.6 1.0
CA A:CYS490 4.5 39.4 1.0
C A:CYS492 4.6 50.8 1.0
C A:LYS451 4.7 56.7 1.0
C A:CYS493 4.7 48.9 1.0
CA A:CYS449 4.8 46.9 1.0
N A:GLY494 4.9 47.0 1.0
CA A:CYS492 4.9 55.4 1.0
N A:CYS492 4.9 50.1 1.0
CA A:LYS451 5.0 57.8 1.0
N A:LYS451 5.0 54.4 1.0

Reference:

L.Pang, S.De Graef, B.Zhang, S.V.Strelkov, A.Van Aerschot, S.D.Weeks. The Essential Role of A Structured Water in Base Recognition of Class II Aminoacyl-Trna Synthetases To Be Published.
Page generated: Wed Oct 30 15:56:02 2024

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