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Magnesium in PDB 5ue7: Crystal Structure of the Phosphomannomutase PMM1 From Candida Albicans, Apoenzyme State

Enzymatic activity of Crystal Structure of the Phosphomannomutase PMM1 From Candida Albicans, Apoenzyme State

All present enzymatic activity of Crystal Structure of the Phosphomannomutase PMM1 From Candida Albicans, Apoenzyme State:
5.4.2.8;

Protein crystallography data

The structure of Crystal Structure of the Phosphomannomutase PMM1 From Candida Albicans, Apoenzyme State, PDB code: 5ue7 was solved by P.J.Stogios, T.Skarina, R.Di Leo, A.Savchenko, W.F.Anderson, Center Forstructural Genomics Of Infectious Diseases (Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.70 / 1.95
Space group P 2 21 21
Cell size a, b, c (Å), α, β, γ (°) 62.225, 80.719, 116.729, 90.00, 90.00, 90.00
R / Rfree (%) 20.8 / 25.7

Other elements in 5ue7:

The structure of Crystal Structure of the Phosphomannomutase PMM1 From Candida Albicans, Apoenzyme State also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Phosphomannomutase PMM1 From Candida Albicans, Apoenzyme State (pdb code 5ue7). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of the Phosphomannomutase PMM1 From Candida Albicans, Apoenzyme State, PDB code: 5ue7:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 5ue7

Go back to Magnesium Binding Sites List in 5ue7
Magnesium binding site 1 out of 4 in the Crystal Structure of the Phosphomannomutase PMM1 From Candida Albicans, Apoenzyme State


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 the Phosphomannomutase PMM1 From Candida Albicans, Apoenzyme State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg301

b:27.4
occ:1.00
 O A:HOH470 2.0 30.4 1.0
O A:HOH417 2.0 29.8 1.0
O A:ASP18 2.0 58.6 1.0
OD2 A:ASP16 2.0 50.6 1.0
OD1 A:ASP213 2.1 52.6 1.0
O A:HOH437 2.3 42.8 1.0
CG A:ASP16 2.9 43.2 1.0
CG A:ASP213 3.0 51.1 1.0
OD1 A:ASP16 3.2 41.4 1.0
C A:ASP18 3.2 56.2 1.0
OD2 A:ASP213 3.3 53.8 1.0
CA A:ASP18 4.1 55.2 1.0
OD2 A:ASP221 4.1 31.0 1.0
CB A:ASP18 4.2 56.7 1.0
OG1 A:THR20 4.2 33.6 1.0
N A:ASP18 4.2 49.1 1.0
CB A:ASP16 4.3 38.0 1.0
N A:GLY19 4.3 55.3 1.0
CB A:ASP213 4.4 47.3 1.0
CG A:LYS214 4.4 43.4 1.0
OD2 A:ASP18 4.4 59.0 1.0
O A:HOH668 4.4 55.3 1.0
O A:HOH622 4.4 52.8 1.0
CA A:GLY19 4.4 52.8 1.0
OD1 A:ASN220 4.5 34.3 1.0
N A:ASP213 4.5 36.5 1.0
N A:THR20 4.7 48.3 1.0
C A:GLY19 4.7 50.5 1.0
CG A:ASP18 4.8 60.0 1.0
O A:HOH509 4.8 36.4 1.0
C A:VAL17 4.9 46.8 1.0
CA A:ASP213 4.9 41.3 1.0
N A:LYS214 4.9 38.7 1.0
OD1 A:ASP221 4.9 28.3 1.0
CG A:ASP221 5.0 28.1 1.0

Magnesium binding site 2 out of 4 in 5ue7

Go back to Magnesium Binding Sites List in 5ue7
Magnesium binding site 2 out of 4 in the Crystal Structure of the Phosphomannomutase PMM1 From Candida Albicans, Apoenzyme State


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 the Phosphomannomutase PMM1 From Candida Albicans, Apoenzyme State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg302

b:23.8
occ:1.00
 O A:TYR225 2.3 30.8 1.0
O A:ASP227 2.6 41.7 1.0
O A:THR230 2.7 34.2 1.0
OG1 A:THR230 2.9 29.7 1.0
C A:THR230 3.4 32.8 1.0
C A:TYR225 3.5 28.6 1.0
N A:ASP227 3.6 35.2 1.0
C A:ASP227 3.7 41.8 1.0
C A:ASN226 3.7 34.9 1.0
CA A:ASN226 3.8 32.1 1.0
CB A:THR230 4.0 29.4 1.0
N A:ASN226 4.0 29.4 1.0
N A:GLY232 4.1 30.0 1.0
CA A:THR230 4.1 32.8 1.0
O A:HOH699 4.2 55.3 1.0
N A:THR230 4.2 37.5 1.0
CA A:ASP227 4.3 38.0 1.0
O A:ASN226 4.3 37.5 1.0
N A:ILE231 4.3 31.6 1.0
O A:ILE224 4.4 23.3 1.0
CA A:ILE231 4.5 32.0 1.0
CA A:TYR225 4.6 25.4 1.0
C A:ILE231 4.6 29.9 1.0
N A:PRO228 4.7 45.6 1.0
CA A:GLY232 4.8 27.8 1.0
CA A:PRO228 4.9 47.5 1.0

Magnesium binding site 3 out of 4 in 5ue7

Go back to Magnesium Binding Sites List in 5ue7
Magnesium binding site 3 out of 4 in the Crystal Structure of the Phosphomannomutase PMM1 From Candida Albicans, Apoenzyme State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of the Phosphomannomutase PMM1 From Candida Albicans, Apoenzyme State within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg301

b:37.6
occ:1.00
 O B:HOH402 1.8 39.8 1.0
OD2 B:ASP16 1.9 66.3 1.0
O B:HOH428 2.0 38.5 1.0
O B:HOH530 2.2 38.6 1.0
O B:ASP18 2.2 74.0 1.0
CG B:ASP16 2.4 58.7 1.0
OD1 B:ASP213 2.5 44.5 1.0
OD1 B:ASP16 2.5 59.0 1.0
C B:ASP18 3.3 70.1 1.0
CG B:ASP213 3.5 46.9 1.0
CB B:ASP16 3.8 51.0 1.0
OD2 B:ASP213 3.9 50.4 1.0
OD2 B:ASP221 4.0 39.0 1.0
N B:ASP18 4.0 62.0 1.0
NZ B:LYS214 4.0 67.6 1.0
CA B:ASP18 4.1 68.5 1.0
OG1 B:THR20 4.1 45.4 1.0
OD1 B:ASN220 4.2 45.4 1.0
CB B:ASP18 4.3 69.9 1.0
O B:HOH587 4.4 35.6 1.0
N B:GLY19 4.4 69.1 1.0
ND2 B:ASN220 4.5 47.5 1.0
O B:HOH592 4.5 58.8 1.0
OD1 B:ASP221 4.5 33.3 1.0
C B:VAL17 4.5 58.6 1.0
CD B:LYS214 4.6 62.8 1.0
N B:VAL17 4.6 49.3 1.0
CA B:GLY19 4.6 65.4 1.0
CG B:ASP221 4.7 36.1 1.0
N B:THR20 4.7 59.5 1.0
N B:ASP213 4.7 39.5 1.0
O B:HOH541 4.8 32.6 1.0
CB B:ASP213 4.8 46.7 1.0
CG B:LYS214 4.8 59.5 1.0
CG B:ASN220 4.8 44.9 1.0
C B:GLY19 4.9 62.5 1.0
CE B:LYS214 4.9 67.8 1.0
C B:ASP16 4.9 49.3 1.0
NZ B:LYS193 4.9 31.6 1.0
CA B:ASP16 4.9 46.8 1.0
CB B:THR20 4.9 48.5 1.0
O B:VAL17 5.0 60.7 1.0

Magnesium binding site 4 out of 4 in 5ue7

Go back to Magnesium Binding Sites List in 5ue7
Magnesium binding site 4 out of 4 in the Crystal Structure of the Phosphomannomutase PMM1 From Candida Albicans, Apoenzyme State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of the Phosphomannomutase PMM1 From Candida Albicans, Apoenzyme State within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg302

b:23.9
occ:1.00
 O B:THR230 2.4 32.6 1.0
O B:TYR225 2.6 33.9 1.0
O B:ASP227 2.7 34.7 1.0
OG1 B:THR230 2.9 33.0 1.0
O B:HOH528 3.1 37.1 1.0
C B:THR230 3.2 33.0 1.0
C B:TYR225 3.7 32.1 1.0
C B:ASP227 3.8 36.6 1.0
C B:ASN226 3.9 35.9 1.0
CA B:THR230 3.9 32.7 1.0
CB B:THR230 4.0 30.8 1.0
N B:ASP227 4.0 35.6 1.0
N B:GLY232 4.0 27.7 1.0
N B:ILE231 4.0 30.9 1.0
N B:THR230 4.1 34.5 1.0
CA B:ASN226 4.1 35.0 1.0
O B:ASN226 4.2 35.4 1.0
CA B:ILE231 4.3 30.7 1.0
N B:ASN226 4.3 32.5 1.0
CA B:ASP227 4.5 34.9 1.0
C B:ILE231 4.5 28.9 1.0
O B:ILE224 4.6 31.9 1.0
O B:HOH547 4.6 40.0 1.0
N B:PRO228 4.7 38.9 1.0
CA B:GLY232 4.8 28.7 1.0
CA B:TYR225 4.8 31.1 1.0
CA B:PRO228 4.8 40.8 1.0

Reference:

P.J.Stogios, P.J.Stogios, T.Skarina, R.Di Leo, A.Savchenko, W.F.Anderson, Center Forstructural Genomics Of Infectious Diseases (Csgid). N/A N/A.
Page generated: Tue Aug 12 20:48:32 2025

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