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Zinc in PDB 2d54: Crystal Structure of Methionyl Trna Synthetase Y225A Mutant From Thermus Thermophilus

Enzymatic activity of Crystal Structure of Methionyl Trna Synthetase Y225A Mutant From Thermus Thermophilus

All present enzymatic activity of Crystal Structure of Methionyl Trna Synthetase Y225A Mutant From Thermus Thermophilus:
6.1.1.10;

Protein crystallography data

The structure of Crystal Structure of Methionyl Trna Synthetase Y225A Mutant From Thermus Thermophilus, PDB code: 2d54 was solved by M.Konno, R.Takeda, R.Takasaka, Y.Mori, R.Ishii, S.Yokoyama, Rikenstructural Genomics/Proteomics Initiative (Rsgi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 50.318, 82.209, 120.560, 90.00, 90.00, 90.00
R / Rfree (%) 20.8 / 25.4

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Methionyl Trna Synthetase Y225A Mutant From Thermus Thermophilus (pdb code 2d54). 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 Crystal Structure of Methionyl Trna Synthetase Y225A Mutant From Thermus Thermophilus, PDB code: 2d54:

Zinc binding site 1 out of 1 in 2d54

Go back to Zinc Binding Sites List in 2d54
Zinc binding site 1 out of 1 in the Crystal Structure of Methionyl Trna Synthetase Y225A Mutant From Thermus Thermophilus


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 Methionyl Trna Synthetase Y225A Mutant From Thermus Thermophilus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1501

b:20.1
occ:1.00
ND1 A:HIS147 2.1 23.6 1.0
SG A:CYS130 2.3 27.0 1.0
SG A:CYS127 2.3 19.6 1.0
SG A:CYS144 2.3 22.9 1.0
CE1 A:HIS147 2.9 21.9 1.0
CG A:HIS147 3.2 24.7 1.0
CB A:CYS130 3.3 24.0 1.0
CB A:CYS127 3.3 17.7 1.0
CB A:CYS144 3.4 25.8 1.0
N A:CYS130 3.6 24.7 1.0
CB A:HIS147 3.7 26.0 1.0
CA A:CYS130 3.9 24.8 1.0
N A:HIS147 4.0 27.6 1.0
NE2 A:HIS147 4.1 20.6 1.0
CB A:ILE146 4.2 27.1 1.0
CD2 A:HIS147 4.3 22.8 1.0
CB A:SER129 4.3 21.8 1.0
CE1 A:TYR134 4.4 26.2 1.0
C A:SER129 4.4 24.7 1.0
OH A:TYR134 4.5 27.2 1.0
CA A:HIS147 4.5 26.6 1.0
CA A:CYS127 4.7 19.5 1.0
CG2 A:ILE146 4.7 25.3 1.0
CA A:CYS144 4.8 27.2 1.0
CA A:SER129 4.8 22.9 1.0
CZ A:TYR134 4.9 27.0 1.0
C A:ILE146 4.9 27.5 1.0
CA A:ILE146 4.9 26.8 1.0
N A:SER129 5.0 21.8 1.0
N A:ILE146 5.0 27.1 1.0
CG1 A:ILE146 5.0 27.6 1.0
O A:CYS127 5.0 19.8 1.0
OG A:SER129 5.0 23.0 1.0

Reference:

M.Konno, R.Takeda, R.Takasaka, Y.Mori, R.Ishii, S.Yokoyama. Y225F/Amutation For Met-Trna Synthetase Reveals Importance of Hydrophobic Circumstance To Be Published.
Page generated: Wed Oct 16 22:36:23 2024

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