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Chlorine in PDB 2cja: Crystal Structure of Methanosarcina Barkeri Seryl-Trna Synthetase Complexed with Atp

Enzymatic activity of Crystal Structure of Methanosarcina Barkeri Seryl-Trna Synthetase Complexed with Atp

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

Protein crystallography data

The structure of Crystal Structure of Methanosarcina Barkeri Seryl-Trna Synthetase Complexed with Atp, PDB code: 2cja 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) 19.74 / 2.2
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 97.314, 97.314, 270.051, 90.00, 90.00, 120.00
R / Rfree (%) 20.3 / 23.3

Other elements in 2cja:

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

Magnesium (Mg) 2 atoms
Zinc (Zn) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Methanosarcina Barkeri Seryl-Trna Synthetase Complexed with Atp (pdb code 2cja). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Methanosarcina Barkeri Seryl-Trna Synthetase Complexed with Atp, PDB code: 2cja:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 2cja

Go back to Chlorine Binding Sites List in 2cja
Chlorine binding site 1 out of 2 in the Crystal Structure of Methanosarcina Barkeri Seryl-Trna Synthetase Complexed with Atp


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Methanosarcina Barkeri Seryl-Trna Synthetase Complexed with Atp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1504

b:34.5
occ:1.00
N A:ALA304 3.1 61.1 1.0
N A:TYR303 3.2 62.3 1.0
NE1 A:TRP245 3.2 60.4 1.0
N A:GLN305 3.5 60.4 1.0
CG2 A:VAL240 3.8 59.6 1.0
CD A:PRO307 3.8 61.4 1.0
CG A:PRO307 3.8 61.1 1.0
CA A:TYR303 3.8 62.3 1.0
C A:TYR303 3.9 62.0 1.0
CA A:ALA304 3.9 60.7 1.0
CB A:TYR303 4.0 62.6 1.0
CD A:PRO308 4.0 61.8 1.0
CE2 A:TRP245 4.0 60.2 1.0
CB A:PRO307 4.1 61.6 1.0
CZ2 A:TRP245 4.1 61.1 1.0
C A:ALA304 4.1 60.5 1.0
CB A:ALA304 4.2 60.0 1.0
C A:CYS302 4.2 62.5 1.0
CD1 A:TRP245 4.3 60.0 1.0
CA A:GLN305 4.3 60.4 1.0
CA A:CYS302 4.3 62.3 1.0
CG1 A:VAL240 4.4 60.2 1.0
CB A:VAL240 4.5 60.6 1.0
C A:GLN305 4.7 60.5 1.0
N A:PRO307 4.7 61.3 1.0
SG A:CYS302 4.8 63.2 1.0
CG A:PRO308 4.8 62.1 1.0

Chlorine binding site 2 out of 2 in 2cja

Go back to Chlorine Binding Sites List in 2cja
Chlorine binding site 2 out of 2 in the Crystal Structure of Methanosarcina Barkeri Seryl-Trna Synthetase Complexed with Atp


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Methanosarcina Barkeri Seryl-Trna Synthetase Complexed with Atp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl1504

b:37.4
occ:1.00
N B:ALA304 3.1 61.0 1.0
N B:TYR303 3.2 62.2 1.0
NE1 B:TRP245 3.2 59.1 1.0
N B:GLN305 3.5 62.3 1.0
CG2 B:VAL240 3.7 58.6 1.0
CD B:PRO307 3.8 61.8 1.0
CG B:PRO307 3.8 61.5 1.0
CA B:TYR303 3.8 62.2 1.0
CB B:TYR303 3.9 63.1 1.0
C B:TYR303 4.0 61.9 1.0
CD B:PRO308 4.0 61.2 1.0
CA B:ALA304 4.0 61.5 1.0
CE2 B:TRP245 4.0 58.8 1.0
CZ2 B:TRP245 4.1 58.6 1.0
C B:ALA304 4.2 61.9 1.0
C B:CYS302 4.2 62.2 1.0
CG1 B:VAL240 4.2 59.7 1.0
CB B:PRO307 4.2 61.9 1.0
CB B:ALA304 4.2 61.2 1.0
CA B:CYS302 4.3 62.0 1.0
CD1 B:TRP245 4.3 58.4 1.0
CA B:GLN305 4.3 62.2 1.0
CB B:VAL240 4.4 58.8 1.0
C B:GLN305 4.8 62.3 1.0
N B:PRO307 4.8 62.2 1.0
CG B:PRO308 4.8 60.9 1.0
SG B:CYS302 4.8 62.8 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: Thu Jul 10 21:45:46 2025

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