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Platinum in PDB 2cim: Crystal Structure of Methanosarcina Barkeri Seryl-Trna Synthetase

Enzymatic activity of Crystal Structure of Methanosarcina Barkeri Seryl-Trna Synthetase

All present enzymatic activity of Crystal Structure of Methanosarcina Barkeri Seryl-Trna Synthetase:
6.1.1.11;

Protein crystallography data

The structure of Crystal Structure of Methanosarcina Barkeri Seryl-Trna Synthetase, PDB code: 2cim was solved by S.Bilokapic, T.Maier, D.Ahel, I.Gruic-Sovulj, D.Soll, I.Weygand-Durasevic, N.Ban, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.94 / 2.51
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 97.150, 97.150, 268.500, 90.00, 90.00, 120.00
R / Rfree (%) 19.9 / 25.2

Other elements in 2cim:

The structure of Crystal Structure of Methanosarcina Barkeri Seryl-Trna Synthetase also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms
Zinc (Zn) 2 atoms

Platinum Binding Sites:

The binding sites of Platinum atom in the Crystal Structure of Methanosarcina Barkeri Seryl-Trna Synthetase (pdb code 2cim). This binding sites where shown within 5.0 Angstroms radius around Platinum atom.
In total only one binding site of Platinum was determined in the Crystal Structure of Methanosarcina Barkeri Seryl-Trna Synthetase, PDB code: 2cim:

Platinum binding site 1 out of 1 in 2cim

Go back to Platinum Binding Sites List in 2cim
Platinum binding site 1 out of 1 in the Crystal Structure of Methanosarcina Barkeri Seryl-Trna Synthetase


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 1 of Crystal Structure of Methanosarcina Barkeri Seryl-Trna Synthetase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Pt1505

b:67.5
occ:0.30
O A:PHE75 4.3 92.5 1.0
CD A:ARG78 4.6 0.7 1.0
CB A:PHE75 4.6 91.7 1.0
CD1 A:PHE75 4.9 91.9 1.0
CG A:PHE75 5.0 91.9 1.0

Reference:

S.Bilokapic, T.Maier, D.Ahel, I.Gruic-Sovulj, D.Soll, I.Weygand-Durasevic, N.Ban. Structure of the Unusual Seryl-Trna Synthetase Reveals A Distinct Zinc-Dependent Mode of Substrate Recognition Embo J. V. 25 2498 2006.
ISSN: ISSN 0261-4189
PubMed: 16675947
DOI: 10.1038/SJ.EMBOJ.7601129
Page generated: Wed Dec 16 02:04:00 2020

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