Atomistry » Magnesium » PDB 5hr6-5i8q » 5hxm
Atomistry »
  Magnesium »
    PDB 5hr6-5i8q »
      5hxm »

Magnesium in PDB 5hxm: Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose

Enzymatic activity of Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose

All present enzymatic activity of Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose:
3.2.1.177;

Protein crystallography data

The structure of Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose, PDB code: 5hxm was solved by A.S.Halavaty, S.H.Light, G.Minasov, J.Winsor, S.Grimshaw, L.Shuvalova, S.Peterson, W.F.Anderson, Center For Structural Genomics Of Infectiousdiseases (Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.74 / 1.90
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 166.157, 102.437, 74.011, 90.00, 103.78, 90.00
R / Rfree (%) 15.2 / 19.5

Other elements in 5hxm:

The structure of Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms
Calcium (Ca) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose (pdb code 5hxm). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 5 binding sites of Magnesium where determined in the Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose, PDB code: 5hxm:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5;

Magnesium binding site 1 out of 5 in 5hxm

Go back to Magnesium Binding Sites List in 5hxm
Magnesium binding site 1 out of 5 in the Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1101

b:42.2
occ:1.00
O A:HOH1502 1.9 45.0 1.0
O A:HOH1300 2.0 37.8 1.0
O A:HOH1536 2.0 40.2 1.0
O A:HOH2067 2.1 40.9 1.0
OD1 A:ASN346 2.1 37.4 1.0
O A:HOH1231 2.1 40.9 1.0
CG A:ASN346 3.1 38.5 1.0
ND2 A:ASN346 3.5 37.8 1.0
O A:HOH1537 3.6 47.7 1.0
OD2 A:ASP349 4.0 48.9 1.0
OD2 A:ASP152 4.0 44.0 1.0
OD2 A:ASP154 4.0 43.2 1.0
OD1 A:ASP342 4.2 45.7 1.0
O A:HOH2053 4.3 55.8 1.0
ND2 A:ASN345 4.3 42.5 1.0
OD2 A:ASP342 4.3 40.8 1.0
OD1 A:ASP154 4.4 43.1 1.0
CB A:ASN346 4.4 35.1 1.0
CG A:ASP342 4.7 44.4 1.0
CG A:ASP154 4.7 43.0 1.0
CA A:ASN346 4.7 36.7 1.0

Magnesium binding site 2 out of 5 in 5hxm

Go back to Magnesium Binding Sites List in 5hxm
Magnesium binding site 2 out of 5 in the Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1102

b:49.0
occ:1.00
O A:HOH1729 2.0 50.0 1.0
O A:HOH1849 2.0 71.2 1.0
OD2 A:ASP376 2.3 47.0 1.0
O A:GLU370 2.3 43.3 1.0
OD1 A:ASP372 2.4 51.0 1.0
O A:HOH1940 2.5 63.4 1.0
CG A:ASP372 3.2 52.0 1.0
CG A:ASP376 3.3 49.7 1.0
C A:GLU370 3.5 46.3 1.0
OD1 A:ASP376 3.7 51.4 1.0
OD2 A:ASP372 3.8 54.8 1.0
N A:ASP372 3.8 45.3 1.0
NE A:ARG373 4.1 56.4 1.0
CB A:ASP372 4.1 50.1 1.0
NH2 A:ARG373 4.3 61.6 1.0
CA A:GLU370 4.4 46.9 1.0
N A:TRP371 4.4 44.2 1.0
CA A:TRP371 4.5 44.8 1.0
CA A:ASP372 4.5 48.9 1.0
CB A:GLU370 4.5 45.0 1.0
O A:SER662 4.6 45.3 1.0
C A:TRP371 4.6 45.0 1.0
CZ A:ARG373 4.6 61.6 1.0
CB A:ASP376 4.6 47.7 1.0
OD1 A:ASP663 4.8 51.1 1.0

Magnesium binding site 3 out of 5 in 5hxm

Go back to Magnesium Binding Sites List in 5hxm
Magnesium binding site 3 out of 5 in the Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1103

b:67.2
occ:1.00
O A:HOH2191 1.8 69.4 1.0
O A:HOH1412 2.2 51.5 1.0
O A:HOH1967 2.2 51.5 1.0
O A:HOH1976 2.3 59.8 1.0
O A:HOH2080 2.4 56.1 1.0
ND2 A:ASN575 4.2 50.6 1.0
OD1 A:ASP529 4.4 49.1 1.0
CG A:ASN575 4.4 50.0 1.0
O A:HOH1286 4.5 44.6 1.0
OD1 A:ASN575 4.5 46.9 1.0
O A:GLY527 4.6 50.7 1.0
CE1 A:HIS444 4.9 52.8 1.0

Magnesium binding site 4 out of 5 in 5hxm

Go back to Magnesium Binding Sites List in 5hxm
Magnesium binding site 4 out of 5 in the Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1104

b:69.4
occ:1.00
O A:HOH2060 1.7 65.9 1.0
O A:HOH2114 2.1 65.7 1.0
O A:HOH2188 2.2 50.2 1.0
O A:HOH2121 2.2 62.9 1.0
O A:HOH1499 2.2 48.0 1.0
O A:HOH2224 2.4 63.3 1.0
O A:HOH1507 3.5 56.7 1.0
O A:HOH1275 4.0 42.6 1.0
O A:HOH2155 4.2 61.0 1.0
O A:HOH1509 4.3 38.2 1.0
O A:HOH1705 4.3 37.9 1.0
NZ A:LYS612 4.4 37.0 1.0
O A:HOH1246 4.6 53.8 1.0
OD2 A:ASP734 4.6 41.6 1.0

Magnesium binding site 5 out of 5 in 5hxm

Go back to Magnesium Binding Sites List in 5hxm
Magnesium binding site 5 out of 5 in the Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Cycloalternan-Forming Enzyme From Listeria Monocytogenes in Complex with Panose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1105

b:85.8
occ:1.00
O A:HOH2150 1.9 69.7 1.0
O A:HOH2055 2.0 76.7 1.0
O A:HOH1325 2.3 55.4 1.0
OD1 A:ASP832 4.1 58.4 1.0
O A:GLU853 4.3 44.0 1.0
OD2 A:ASP832 4.4 64.8 1.0
O A:HOH1547 4.4 55.8 1.0
CG A:ASP832 4.5 56.4 1.0
CA A:GLY831 4.9 47.0 1.0

Reference:

S.H.Light, L.A.Cahoon, K.V.Mahasenan, M.Lee, B.Boggess, A.S.Halavaty, S.Mobashery, N.E.Freitag, W.F.Anderson. Transferase Versus Hydrolase: the Role of Conformational Flexibility in Reaction Specificity. Structure V. 25 295 2017.
ISSN: ISSN 1878-4186
PubMed: 28089449
DOI: 10.1016/J.STR.2016.12.007
Page generated: Sun Sep 29 16:36:39 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy