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Magnesium in PDB 3zvi: Methylaspartate Ammonia Lyase From Clostridium Tetanomorphum Mutant L384A

Enzymatic activity of Methylaspartate Ammonia Lyase From Clostridium Tetanomorphum Mutant L384A

All present enzymatic activity of Methylaspartate Ammonia Lyase From Clostridium Tetanomorphum Mutant L384A:
4.3.1.2;

Protein crystallography data

The structure of Methylaspartate Ammonia Lyase From Clostridium Tetanomorphum Mutant L384A, PDB code: 3zvi was solved by H.Raj, W.Szymanski, J.De Villiers, H.J.Rozeboom, V.P.Veetil, C.R.Reis, M.Devilliers, S.De Wildeman, F.J.Dekker, W.J.Quax, A.M.W.H.Thunnissen, B.L.Feringa, D.B.Janssen, G.J.Poelarends, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.03 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 66.621, 109.863, 110.853, 90.00, 90.00, 90.00
R / Rfree (%) 16 / 21

Other elements in 3zvi:

The structure of Methylaspartate Ammonia Lyase From Clostridium Tetanomorphum Mutant L384A also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Methylaspartate Ammonia Lyase From Clostridium Tetanomorphum Mutant L384A (pdb code 3zvi). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Methylaspartate Ammonia Lyase From Clostridium Tetanomorphum Mutant L384A, PDB code: 3zvi:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 3zvi

Go back to Magnesium Binding Sites List in 3zvi
Magnesium binding site 1 out of 2 in the Methylaspartate Ammonia Lyase From Clostridium Tetanomorphum Mutant L384A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Methylaspartate Ammonia Lyase From Clostridium Tetanomorphum Mutant L384A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1421

b:13.8
occ:1.00
OE2 A:GLU273 2.0 12.6 1.0
O A:HOH2297 2.0 13.9 1.0
OD2 A:ASP307 2.0 14.3 1.0
O A:HOH2296 2.0 9.1 1.0
OD2 A:ASP238 2.1 13.4 1.0
O A:HOH2261 2.1 12.6 1.0
CD A:GLU273 3.0 12.6 1.0
CG A:ASP307 3.1 12.6 1.0
CG A:ASP238 3.1 10.8 1.0
OD1 A:ASP238 3.4 10.5 1.0
CB A:ASP307 3.5 12.6 1.0
CG A:GLU273 3.6 10.4 1.0
OE1 A:GLU273 3.9 14.7 1.0
OE1 A:GLN329 4.0 18.3 1.0
O A:HOH2354 4.1 22.1 1.0
O A:HOH2262 4.1 6.3 1.0
OE2 A:GLU308 4.2 17.7 1.0
OD1 A:ASP307 4.2 14.9 1.0
OE1 A:GLU308 4.4 13.2 1.0
CB A:ASP238 4.4 11.1 1.0
NE2 A:HIS194 4.5 13.6 1.0
CD A:GLU308 4.6 16.0 1.0
CB A:GLU273 4.7 10.7 1.0
CZ A:TYR240 4.8 19.7 1.0

Magnesium binding site 2 out of 2 in 3zvi

Go back to Magnesium Binding Sites List in 3zvi
Magnesium binding site 2 out of 2 in the Methylaspartate Ammonia Lyase From Clostridium Tetanomorphum Mutant L384A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Methylaspartate Ammonia Lyase From Clostridium Tetanomorphum Mutant L384A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1421

b:12.3
occ:1.00
OE2 B:GLU273 1.9 11.6 1.0
OD2 B:ASP238 2.0 7.2 1.0
OD2 B:ASP307 2.0 8.0 1.0
O B:HOH2214 2.1 7.4 1.0
O B:HOH2254 2.1 12.9 1.0
O B:HOH2253 2.2 9.0 1.0
CD B:GLU273 3.0 10.7 1.0
CG B:ASP307 3.0 9.7 1.0
CG B:ASP238 3.1 7.7 1.0
CB B:ASP307 3.4 8.3 1.0
OD1 B:ASP238 3.5 8.6 1.0
CG B:GLU273 3.6 8.3 1.0
OE1 B:GLU273 4.0 12.2 1.0
OE2 B:GLU308 4.0 17.6 1.0
OE1 B:GLN329 4.1 16.9 1.0
OD1 B:ASP307 4.2 9.3 1.0
OE1 B:GLU308 4.3 11.2 1.0
CB B:ASP238 4.3 8.1 1.0
NE2 B:HIS194 4.4 11.5 1.0
O B:HOH2190 4.5 3.4 1.0
CD B:GLU308 4.6 13.6 1.0
CZ B:TYR240 4.7 17.8 1.0
CB B:GLU273 4.8 8.1 1.0
OH B:TYR240 4.9 18.3 1.0
CE2 B:TYR240 4.9 16.6 1.0
CA B:ASP307 5.0 8.7 1.0

Reference:

H.Raj, W.Szymanski, J.De Villiers, H.J.Rozeboom, V.P.Veetil, C.R.Reis, M.De Villiers, F.J.Dekker, S.De Wildeman, W.J.Quax, A.M.W.H.Thunnissen, B.L.Feringa, D.B.Janssen, G.J.Poelarends. Engineering Methylaspartate Ammonia Lyase For the Asymmetric Synthesis of Unnatural Amino Acids. Nat.Chem. V. 4 478 2012.
ISSN: ISSN 1755-4330
PubMed: 22614383
DOI: 10.1038/NCHEM.1338
Page generated: Mon Dec 14 09:04:35 2020

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