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

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

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

Protein crystallography data

The structure of Crystal Structure of Methanosarcina Barkeri Seryl-Trna Synthetase Complexed with Serine, PDB code: 2cjb 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 / 2.70
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 96.933, 96.933, 270.503, 90.00, 90.00, 120.00
R / Rfree (%) 21.7 / 27.2

Other elements in 2cjb:

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

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 Serine (pdb code 2cjb). 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 Serine, PDB code: 2cjb:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 2cjb

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


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 Serine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1504

b:56.9
occ:1.00
NE1 A:TRP245 3.0 92.7 1.0
N A:ALA304 3.1 94.3 1.0
N A:TYR303 3.4 92.4 1.0
N A:GLN305 3.5 95.9 1.0
CG A:PRO307 3.8 96.4 1.0
CE2 A:TRP245 3.8 93.5 1.0
CG2 A:VAL240 3.9 96.3 1.0
CA A:TYR303 3.9 92.6 1.0
CB A:TYR303 3.9 92.1 1.0
CA A:ALA304 3.9 95.0 1.0
CB A:PRO307 4.0 95.7 1.0
CZ2 A:TRP245 4.0 92.9 1.0
CD A:PRO307 4.0 96.7 1.0
C A:TYR303 4.0 93.2 1.0
CB A:ALA304 4.0 95.0 1.0
CD A:PRO308 4.1 93.0 1.0
CD1 A:TRP245 4.1 92.8 1.0
C A:ALA304 4.1 95.5 1.0
CA A:GLN305 4.4 95.9 1.0
C A:CYS302 4.4 93.0 1.0
CA A:CYS302 4.5 93.3 1.0
CB A:VAL240 4.7 95.6 1.0
CG1 A:VAL240 4.7 96.0 1.0
C A:GLN305 4.8 96.5 1.0
N A:PRO307 4.8 96.7 1.0
CG A:PRO308 4.9 92.5 1.0
SG A:CYS302 4.9 92.2 1.0

Chlorine binding site 2 out of 2 in 2cjb

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


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 Serine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl1504

b:58.6
occ:1.00
N B:ALA304 3.1 93.5 1.0
NE1 B:TRP245 3.2 86.2 1.0
N B:TYR303 3.4 92.8 1.0
CG B:PRO307 3.5 97.5 1.0
N B:GLN305 3.6 96.0 1.0
CD B:PRO307 3.7 97.6 1.0
CB B:PRO307 3.8 97.2 1.0
CA B:ALA304 3.9 93.9 1.0
CG2 B:VAL240 3.9 90.8 1.0
CA B:TYR303 3.9 92.5 1.0
CB B:TYR303 3.9 92.0 1.0
CB B:ALA304 3.9 93.1 1.0
C B:TYR303 4.0 93.0 1.0
CE2 B:TRP245 4.0 86.8 1.0
CZ2 B:TRP245 4.1 87.0 1.0
C B:ALA304 4.2 94.9 1.0
CD1 B:TRP245 4.2 86.0 1.0
CD B:PRO308 4.3 95.7 1.0
C B:CYS302 4.4 93.1 1.0
CG1 B:VAL240 4.4 91.5 1.0
CA B:CYS302 4.4 93.3 1.0
CG B:PRO308 4.5 96.0 1.0
CB B:VAL240 4.6 90.9 1.0
CA B:GLN305 4.6 96.9 1.0
N B:PRO307 4.7 98.1 1.0
CA B:PRO307 4.9 97.4 1.0
SG B:CYS302 5.0 93.9 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: Thu Jul 10 21:45:50 2025

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