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Magnesium in PDB 2iht: Carboxyethylarginine Synthase From Streptomyces Clavuligerus: Semet Structure

Enzymatic activity of Carboxyethylarginine Synthase From Streptomyces Clavuligerus: Semet Structure

All present enzymatic activity of Carboxyethylarginine Synthase From Streptomyces Clavuligerus: Semet Structure:
2.5.1.66;

Protein crystallography data

The structure of Carboxyethylarginine Synthase From Streptomyces Clavuligerus: Semet Structure, PDB code: 2iht was solved by M.E.Caines, C.J.Schofield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.26 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 117.882, 127.279, 197.328, 90.00, 90.00, 90.00
R / Rfree (%) 15.4 / 17.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Carboxyethylarginine Synthase From Streptomyces Clavuligerus: Semet Structure (pdb code 2iht). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Carboxyethylarginine Synthase From Streptomyces Clavuligerus: Semet Structure, PDB code: 2iht:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 2iht

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Magnesium binding site 1 out of 4 in the Carboxyethylarginine Synthase From Streptomyces Clavuligerus: Semet Structure


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Carboxyethylarginine Synthase From Streptomyces Clavuligerus: Semet Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg601

b:2.6
occ:1.00
 O3B A:TPP600 2.1 10.1 1.0
OD1 A:ASN490 2.2 13.7 1.0
OD1 A:ASP463 2.2 10.1 1.0
O1A A:TPP600 2.2 10.2 1.0
O A:THR492 2.2 10.5 1.0
O A:HOH793 2.3 13.7 1.0
CG A:ASP463 3.3 9.9 1.0
CG A:ASN490 3.4 13.2 1.0
PB A:TPP600 3.4 11.8 1.0
PA A:TPP600 3.4 9.6 1.0
C A:THR492 3.4 10.6 1.0
O3A A:TPP600 3.7 11.5 1.0
OD2 A:ASP463 3.8 9.9 1.0
N A:GLY494 3.9 9.5 1.0
O7 A:TPP600 4.0 10.8 1.0
N A:THR492 4.0 11.2 1.0
N A:ASN490 4.1 12.2 1.0
O1B A:TPP600 4.1 13.4 1.0
N A:ASP463 4.1 9.9 1.0
ND2 A:ASN490 4.2 14.9 1.0
CA A:THR492 4.2 10.9 1.0
N A:GLY464 4.3 9.3 1.0
CB A:ASN490 4.4 12.5 1.0
N A:ASN493 4.5 10.2 1.0
O A:VAL488 4.5 11.1 1.0
CB A:ASP463 4.5 9.7 1.0
O2B A:TPP600 4.5 11.6 1.0
CA A:ASN490 4.6 12.3 1.0
CB A:THR492 4.6 10.9 1.0
CA A:ASN493 4.6 9.7 1.0
O2A A:TPP600 4.7 10.6 1.0
CA A:GLY494 4.7 9.4 1.0
C A:ASN490 4.7 12.2 1.0
N A:ASP491 4.7 12.0 1.0
CA A:ASP463 4.7 9.5 1.0
C A:ASN493 4.8 9.4 1.0
CE2 A:TYR561 4.8 21.9 1.0
OH A:TYR561 4.8 22.2 1.0
C A:GLY462 4.8 10.0 1.0
CA A:GLY462 4.8 10.0 1.0

Magnesium binding site 2 out of 4 in 2iht

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Magnesium binding site 2 out of 4 in the Carboxyethylarginine Synthase From Streptomyces Clavuligerus: Semet Structure


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Carboxyethylarginine Synthase From Streptomyces Clavuligerus: Semet Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg601

b:2.4
occ:1.00
 O B:HOH913 2.2 12.2 1.0
OD1 B:ASN490 2.2 13.4 1.0
O3B B:TPP600 2.2 11.2 1.0
O1A B:TPP600 2.3 9.5 1.0
OD1 B:ASP463 2.3 10.6 1.0
O B:THR492 2.3 10.3 1.0
CG B:ASP463 3.3 10.0 1.0
CG B:ASN490 3.4 13.2 1.0
PA B:TPP600 3.4 9.4 1.0
PB B:TPP600 3.4 11.4 1.0
C B:THR492 3.5 10.7 1.0
O3A B:TPP600 3.7 11.2 1.0
OD2 B:ASP463 3.8 10.6 1.0
O7 B:TPP600 4.0 10.3 1.0
N B:GLY494 4.0 9.2 1.0
N B:THR492 4.1 11.6 1.0
N B:ASP463 4.1 9.9 1.0
N B:ASN490 4.1 12.5 1.0
O1B B:TPP600 4.1 12.9 1.0
ND2 B:ASN490 4.2 14.6 1.0
CA B:THR492 4.3 11.1 1.0
N B:GLY464 4.3 9.8 1.0
O B:VAL488 4.4 11.4 1.0
CB B:ASN490 4.4 12.5 1.0
N B:ASN493 4.5 10.2 1.0
CB B:ASP463 4.5 10.1 1.0
CA B:ASN490 4.6 12.5 1.0
CB B:THR492 4.6 11.3 1.0
O2B B:TPP600 4.7 10.6 1.0
O2A B:TPP600 4.7 8.1 1.0
CA B:ASN493 4.7 9.8 1.0
OH B:TYR561 4.7 22.1 1.0
C B:ASN490 4.7 12.3 1.0
N B:ASP491 4.7 12.5 1.0
CA B:ASP463 4.7 10.0 1.0
CA B:GLY494 4.8 9.4 1.0
CA B:GLY462 4.8 9.8 1.0
C B:GLY462 4.8 10.1 1.0
CE2 B:TYR561 4.8 22.1 1.0
C B:ASN493 4.9 9.6 1.0

Magnesium binding site 3 out of 4 in 2iht

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Magnesium binding site 3 out of 4 in the Carboxyethylarginine Synthase From Streptomyces Clavuligerus: Semet Structure


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Carboxyethylarginine Synthase From Streptomyces Clavuligerus: Semet Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg601

b:2.0
occ:1.00
 O1A C:TPP600 2.2 9.8 1.0
OD1 C:ASN490 2.2 13.1 1.0
O C:HOH834 2.2 11.1 1.0
OD1 C:ASP463 2.3 11.0 1.0
O3B C:TPP600 2.3 10.9 1.0
O C:THR492 2.3 10.5 1.0
CG C:ASP463 3.3 10.1 1.0
PA C:TPP600 3.4 9.1 1.0
CG C:ASN490 3.4 13.5 1.0
PB C:TPP600 3.5 12.2 1.0
C C:THR492 3.5 10.7 1.0
O3A C:TPP600 3.7 11.4 1.0
OD2 C:ASP463 3.7 10.4 1.0
O7 C:TPP600 4.0 10.5 1.0
N C:GLY494 4.0 9.7 1.0
N C:THR492 4.0 11.9 1.0
N C:ASN490 4.1 12.5 1.0
N C:ASP463 4.1 10.1 1.0
ND2 C:ASN490 4.2 14.5 1.0
O1B C:TPP600 4.2 13.0 1.0
CA C:THR492 4.3 11.2 1.0
N C:GLY464 4.3 9.6 1.0
OH C:TYR561 4.4 22.0 1.0
CB C:ASN490 4.4 12.6 1.0
O C:VAL488 4.5 11.3 1.0
N C:ASN493 4.5 10.3 1.0
CB C:ASP463 4.5 9.9 1.0
CA C:ASN490 4.6 12.6 1.0
CE2 C:TYR561 4.6 22.4 1.0
CB C:THR492 4.6 11.3 1.0
O2A C:TPP600 4.6 9.7 1.0
O2B C:TPP600 4.7 12.0 1.0
CA C:ASN493 4.7 10.0 1.0
C C:ASN490 4.7 12.4 1.0
N C:ASP491 4.7 12.6 1.0
CA C:GLY494 4.7 9.6 1.0
CA C:ASP463 4.8 9.9 1.0
CA C:GLY462 4.8 10.5 1.0
C C:GLY462 4.8 10.5 1.0
C C:ASN493 4.9 9.8 1.0

Magnesium binding site 4 out of 4 in 2iht

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Magnesium binding site 4 out of 4 in the Carboxyethylarginine Synthase From Streptomyces Clavuligerus: Semet Structure


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Carboxyethylarginine Synthase From Streptomyces Clavuligerus: Semet Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg601

b:2.3
occ:1.00
 OD1 D:ASN490 2.2 13.2 1.0
O D:HOH2106 2.2 12.6 1.0
O3B D:TPP600 2.2 10.6 1.0
OD1 D:ASP463 2.3 10.8 1.0
O1A D:TPP600 2.3 10.1 1.0
O D:THR492 2.3 10.7 1.0
CG D:ASP463 3.3 9.6 1.0
CG D:ASN490 3.4 13.5 1.0
PA D:TPP600 3.4 10.3 1.0
PB D:TPP600 3.5 10.8 1.0
C D:THR492 3.5 10.6 1.0
O3A D:TPP600 3.7 10.2 1.0
OD2 D:ASP463 3.8 10.1 1.0
N D:ASN490 4.0 12.3 1.0
N D:ASP463 4.0 9.4 1.0
N D:THR492 4.0 11.1 1.0
O7 D:TPP600 4.0 10.8 1.0
N D:GLY494 4.1 10.0 1.0
ND2 D:ASN490 4.2 14.8 1.0
O1B D:TPP600 4.2 12.6 1.0
CA D:THR492 4.3 10.8 1.0
N D:GLY464 4.3 8.8 1.0
O D:VAL488 4.4 11.3 1.0
CB D:ASN490 4.4 12.6 1.0
CB D:ASP463 4.5 9.7 1.0
CA D:ASN490 4.5 12.6 1.0
N D:ASN493 4.6 10.2 1.0
OH D:TYR561 4.6 22.8 1.0
N D:ASP491 4.6 12.2 1.0
O2A D:TPP600 4.6 9.1 1.0
C D:ASN490 4.7 12.3 1.0
CB D:THR492 4.7 10.9 1.0
O2B D:TPP600 4.7 12.0 1.0
CA D:ASP463 4.7 9.3 1.0
CA D:ASN493 4.7 10.0 1.0
CA D:GLY494 4.8 9.9 1.0
CE2 D:TYR561 4.8 22.3 1.0
CA D:GLY462 4.8 9.6 1.0
C D:GLY462 4.8 9.7 1.0
C D:ASN493 4.9 10.0 1.0

Reference:

M.E.Caines, J.L.Sorensen, C.J.Schofield. Structural and Mechanistic Studies on N(2)-(2-Carboxyethyl)Arginine Synthase. Biochem.Biophys.Res.Commun. V. 385 512 2009.
ISSN: ISSN 0006-291X
PubMed: 19477162
DOI: 10.1016/J.BBRC.2009.05.095
Page generated: Mon Dec 14 07:27:19 2020

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