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Zinc in PDB 3vu8: Metionyl-Trna Synthetase From Thermus Thermophilus Complexed with Methionyl-Adenylate Analogue

Enzymatic activity of Metionyl-Trna Synthetase From Thermus Thermophilus Complexed with Methionyl-Adenylate Analogue

All present enzymatic activity of Metionyl-Trna Synthetase From Thermus Thermophilus Complexed with Methionyl-Adenylate Analogue:
6.1.1.10;

Protein crystallography data

The structure of Metionyl-Trna Synthetase From Thermus Thermophilus Complexed with Methionyl-Adenylate Analogue, PDB code: 3vu8 was solved by M.Konno, M.Kato-Murayama, S.Toma-Fukai, E.Uchikawa, O.Nureki, S.Yokoyama, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 50.823, 82.682, 120.165, 90.00, 90.00, 90.00
R / Rfree (%) 20 / 30

Zinc Binding Sites:

The binding sites of Zinc atom in the Metionyl-Trna Synthetase From Thermus Thermophilus Complexed with Methionyl-Adenylate Analogue (pdb code 3vu8). 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 Metionyl-Trna Synthetase From Thermus Thermophilus Complexed with Methionyl-Adenylate Analogue, PDB code: 3vu8:

Zinc binding site 1 out of 1 in 3vu8

Go back to Zinc Binding Sites List in 3vu8
Zinc binding site 1 out of 1 in the Metionyl-Trna Synthetase From Thermus Thermophilus Complexed with Methionyl-Adenylate Analogue


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Metionyl-Trna Synthetase From Thermus Thermophilus Complexed with Methionyl-Adenylate Analogue within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn601

b:53.1
occ:1.00
 SG A:CYS127 2.1 39.9 1.0
SG A:CYS130 2.4 37.2 1.0
ND1 A:HIS147 2.4 31.9 1.0
SG A:CYS144 2.6 32.1 1.0
CG A:HIS147 3.1 33.6 1.0
CB A:CYS130 3.2 29.5 1.0
CB A:CYS127 3.2 37.3 1.0
CB A:HIS147 3.3 37.0 1.0
CE1 A:HIS147 3.4 31.8 1.0
N A:CYS130 3.5 27.6 1.0
CB A:CYS144 3.6 41.1 1.0
CA A:CYS130 3.8 28.1 1.0
N A:HIS147 4.1 45.0 1.0
CB A:SER129 4.2 30.1 1.0
CD2 A:HIS147 4.2 34.6 1.0
C A:SER129 4.2 31.3 1.0
NE2 A:HIS147 4.3 37.2 1.0
CA A:HIS147 4.3 42.2 1.0
NE A:ARG149 4.3 71.5 1.0
CA A:CYS127 4.6 35.4 1.0
CA A:SER129 4.6 32.3 1.0
N A:SER129 4.7 29.8 1.0
NH2 A:ARG149 4.7 75.0 1.0
C A:CYS127 4.9 33.4 1.0
CB A:ILE146 4.9 45.2 1.0
CZ A:ARG149 4.9 75.9 1.0
C A:ILE146 4.9 46.6 1.0
CG A:ARG149 5.0 63.3 1.0
CA A:CYS144 5.0 47.6 1.0
O A:SER129 5.0 34.8 1.0

Reference:

M.Konno, M.Kato-Murayama, R.Takeda, R.Takasaka, E.Uchikawa, S.Toma-Fukai, R.Ishii, O.Nureki, S.Yokoyama. The Modeling of Structures of Specific Conformation of Homosysteine-Amp Leading to Thiolactone-Formation on Class Ia Aminoacyl-Trna Synthetases To Be Published.
Page generated: Sat Oct 26 17:53:24 2024

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