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Magnesium 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:

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

Magnesium Binding Sites:

The binding sites of Magnesium 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 Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Methanosarcina Barkeri Seryl-Trna Synthetase Complexed with Atp, PDB code: 2cja:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 2cja

Go back to Magnesium Binding Sites List in 2cja
Magnesium 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 Magnesium with other atoms in the Mg 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
B:Mg1505

b:70.6
occ:1.00
OE2 B:GLU338 2.7 74.3 1.0
N7 B:ATP1507 3.0 50.5 1.0
O3G B:ATP1507 3.0 78.3 1.0
NH1 B:ARG336 3.0 64.6 1.0
O2B B:ATP1507 3.1 74.9 1.0
CD B:GLU338 3.6 72.8 1.0
CD B:ARG336 3.6 65.6 1.0
OE1 B:GLU338 3.7 75.7 1.0
C8 B:ATP1507 3.9 50.8 1.0
C5 B:ATP1507 3.9 50.4 1.0
N6 B:ATP1507 4.0 50.7 1.0
CZ B:ARG336 4.1 66.7 1.0
PB B:ATP1507 4.2 75.5 1.0
PG B:ATP1507 4.3 78.8 1.0
NE B:ARG336 4.3 66.3 1.0
O3A B:ATP1507 4.3 73.1 1.0
NH2 B:ARG347 4.3 82.0 1.0
O3B B:ATP1507 4.4 76.6 1.0
C6 B:ATP1507 4.4 50.5 1.0
NH2 B:ARG468 4.5 67.0 1.0
NH1 B:ARG347 4.6 82.0 1.0
OE2 B:GLU257 4.7 74.0 1.0
CZ B:ARG347 4.7 80.7 1.0
O1G B:ATP1507 4.8 78.4 1.0
CG B:ARG336 4.9 65.6 1.0
O1A B:ATP1507 4.9 70.0 1.0
CB B:ARG336 5.0 63.3 1.0

Magnesium binding site 2 out of 2 in 2cja

Go back to Magnesium Binding Sites List in 2cja
Magnesium 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 Magnesium with other atoms in the Mg 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:Mg1506

b:76.6
occ:1.00
OD1 B:ASP416 2.6 71.7 1.0
O2A B:ATP1507 2.6 71.2 1.0
OE1 B:GLU432 2.6 74.4 1.0
OD1 B:ASN435 2.9 74.1 1.0
CB B:ASN435 3.3 67.1 1.0
O1B B:ATP1507 3.3 75.0 1.0
CG B:ASN435 3.4 70.0 1.0
CG B:ASP416 3.5 70.0 1.0
O B:HOH2230 3.5 76.3 1.0
OD2 B:ASP416 3.6 72.9 1.0
CD B:GLU432 3.8 73.4 1.0
CG2 B:THR414 3.8 67.4 1.0
PA B:ATP1507 4.0 69.8 1.0
CG B:GLU432 4.3 69.9 1.0
O3A B:ATP1507 4.4 73.1 1.0
PB B:ATP1507 4.4 75.5 1.0
O3' B:ATP1507 4.6 59.9 1.0
ND2 B:ASN435 4.7 71.5 1.0
CA B:ASN435 4.7 66.7 1.0
C5' B:ATP1507 4.8 62.6 1.0
OE2 B:GLU432 4.8 76.9 1.0
CB B:ASP416 4.9 67.5 1.0
O5' B:ATP1507 5.0 67.1 1.0
O3B B:ATP1507 5.0 76.6 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: Mon Dec 14 07:19:12 2020

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