Atomistry » Magnesium » PDB 3c5i-3cf5 » 3caw
Atomistry »
  Magnesium »
    PDB 3c5i-3cf5 »
      3caw »

Magnesium in PDB 3caw: Crystal Structure of O-Succinylbenzoate Synthase From Bdellovibrio Bacteriovorus Liganded with Mg

Protein crystallography data

The structure of Crystal Structure of O-Succinylbenzoate Synthase From Bdellovibrio Bacteriovorus Liganded with Mg, PDB code: 3caw was solved by A.A.Fedorov, E.V.Fedorov, A.Sakai, S.K.Burley, J.A.Gerlt, S.C.Almo, Newyork Sgx Research Center For Structural Genomics (Nysgxrc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.85 / 1.87
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 53.381, 78.610, 78.462, 90.00, 91.78, 90.00
R / Rfree (%) 21.8 / 24.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of O-Succinylbenzoate Synthase From Bdellovibrio Bacteriovorus Liganded with Mg (pdb code 3caw). 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 O-Succinylbenzoate Synthase From Bdellovibrio Bacteriovorus Liganded with Mg, PDB code: 3caw:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 3caw

Go back to Magnesium Binding Sites List in 3caw
Magnesium binding site 1 out of 2 in the Crystal Structure of O-Succinylbenzoate Synthase From Bdellovibrio Bacteriovorus Liganded with Mg


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 O-Succinylbenzoate Synthase From Bdellovibrio Bacteriovorus Liganded with Mg within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg401

b:28.8
occ:1.00
OD2 A:ASP206 2.3 21.1 1.0
OE1 A:GLU184 2.3 24.7 1.0
OD2 A:ASP155 2.3 26.1 1.0
O A:HOH519 2.3 31.3 1.0
O A:HOH518 2.4 26.7 1.0
O A:HOH517 2.5 30.7 1.0
CG A:ASP155 3.2 22.4 1.0
CD A:GLU184 3.3 22.4 1.0
CG A:ASP206 3.3 22.0 1.0
OD1 A:ASP155 3.4 23.9 1.0
OE2 A:GLU184 3.7 25.1 1.0
CB A:ASP206 3.7 17.2 1.0
NZ A:LYS128 4.2 28.0 1.0
ND2 A:ASN157 4.3 31.9 1.0
NZ A:LYS228 4.3 35.1 1.0
OD2 A:ASP185 4.4 20.2 1.0
OD1 A:ASP206 4.4 24.4 1.0
CB A:GLU184 4.5 16.5 1.0
CG A:GLU184 4.5 20.3 1.0
CB A:ASP155 4.5 20.6 1.0
CE A:LYS128 4.6 27.3 1.0
CE A:LYS228 4.8 33.4 1.0

Magnesium binding site 2 out of 2 in 3caw

Go back to Magnesium Binding Sites List in 3caw
Magnesium binding site 2 out of 2 in the Crystal Structure of O-Succinylbenzoate Synthase From Bdellovibrio Bacteriovorus Liganded with Mg


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 O-Succinylbenzoate Synthase From Bdellovibrio Bacteriovorus Liganded with Mg within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg401

b:29.3
occ:1.00
OD2 B:ASP155 2.3 28.4 1.0
OD2 B:ASP206 2.4 25.2 1.0
OE1 B:GLU184 2.4 32.2 1.0
O B:HOH524 2.4 27.7 1.0
O B:HOH523 2.4 30.6 1.0
O B:HOH525 2.5 30.2 1.0
CG B:ASP155 3.1 25.8 1.0
CG B:ASP206 3.3 24.2 1.0
OD1 B:ASP155 3.4 28.0 1.0
CD B:GLU184 3.4 30.1 1.0
CB B:ASP206 3.8 20.1 1.0
OE2 B:GLU184 4.1 32.3 1.0
OD1 B:ASN157 4.2 33.5 1.0
NZ B:LYS128 4.2 33.1 1.0
CB B:ASP155 4.3 20.7 1.0
O B:HOH510 4.4 37.1 1.0
OD1 B:ASP206 4.4 26.3 1.0
CB B:GLU184 4.4 22.6 1.0
OD2 B:ASP185 4.4 26.2 1.0
CG B:GLU184 4.5 28.4 1.0
CE B:LYS128 4.8 33.0 1.0
CG B:ASN157 5.0 31.4 1.0

Reference:

D.Odokonyero, A.Sakai, Y.Patskovsky, V.N.Malashkevich, A.A.Fedorov, J.B.Bonanno, E.V.Fedorov, R.Toro, R.Agarwal, C.Wang, N.D.Ozerova, W.S.Yew, J.M.Sauder, S.Swaminathan, S.K.Burley, S.C.Almo, M.E.Glasner. Loss of Quaternary Structure Is Associated with Rapid Sequence Divergence in the Osbs Family. Proc.Natl.Acad.Sci.Usa V. 111 8535 2014.
ISSN: ISSN 0027-8424
PubMed: 24872444
DOI: 10.1073/PNAS.1318703111
Page generated: Wed Aug 14 09:32:23 2024

Last articles

Cl in 3QQ8
Cl in 3QQ7
Cl in 3QP5
Cl in 3QPX
Cl in 3QPJ
Cl in 3QPK
Cl in 3QPW
Cl in 3QPG
Cl in 3QM1
Cl in 3QOO
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy