Magnesium in PDB 6i5x: Crystal Structure of Aspergillus Fumigatus Phosphomannomutase

Enzymatic activity of Crystal Structure of Aspergillus Fumigatus Phosphomannomutase

All present enzymatic activity of Crystal Structure of Aspergillus Fumigatus Phosphomannomutase:
5.4.2.8;

Protein crystallography data

The structure of Crystal Structure of Aspergillus Fumigatus Phosphomannomutase, PDB code: 6i5x was solved by Y.Zhang, O.G.Raimi, A.T.Ferenbach, D.M.F.Van Aalten, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.60 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 80.425, 102.024, 137.791, 90.00, 90.00, 90.00
R / Rfree (%) 19.8 / 24.4

Other elements in 6i5x:

The structure of Crystal Structure of Aspergillus Fumigatus Phosphomannomutase also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Aspergillus Fumigatus Phosphomannomutase (pdb code 6i5x). 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 Aspergillus Fumigatus Phosphomannomutase, PDB code: 6i5x:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 6i5x

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Magnesium binding site 1 out of 4 in the Crystal Structure of Aspergillus Fumigatus Phosphomannomutase


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 Aspergillus Fumigatus Phosphomannomutase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg301

b:16.5
occ:1.00
 O A:HOH411 1.9 16.6 1.0
O A:HOH418 2.0 8.8 1.0
OD2 A:ASP20 2.1 14.6 1.0
OD1 A:ASP226 2.1 16.7 1.0
O A:ASP22 2.2 16.5 1.0
O A:HOH425 2.2 18.1 1.0
CG A:ASP20 3.0 15.5 1.0
CG A:ASP226 3.2 17.8 1.0
OD1 A:ASP20 3.3 15.7 1.0
C A:ASP22 3.4 17.4 1.0
OD2 A:ASP226 3.5 18.6 1.0
CA A:ASP22 4.1 18.0 1.0
OD2 A:ASP234 4.1 14.9 1.0
N A:ASP22 4.2 16.6 1.0
CB A:ASP22 4.2 19.9 1.0
OG1 A:THR24 4.3 16.3 1.0
CB A:ASP20 4.4 14.3 1.0
N A:GLU23 4.4 18.5 1.0
CB A:ASP226 4.5 16.6 1.0
CB A:GLU23 4.5 22.4 1.0
CG A:LYS227 4.6 23.0 1.0
N A:ASP226 4.7 16.4 1.0
O A:HOH564 4.7 14.6 1.0
CA A:GLU23 4.8 19.8 1.0
O A:HOH529 4.8 18.5 1.0
C A:GLU23 4.9 19.2 1.0
C A:VAL21 4.9 17.6 1.0
NZ A:LYS200 4.9 24.8 1.0
OD1 A:ASN233 5.0 29.5 1.0
N A:THR24 5.0 18.2 1.0
CG A:ASP234 5.0 15.1 1.0

Magnesium binding site 2 out of 4 in 6i5x

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Magnesium binding site 2 out of 4 in the Crystal Structure of Aspergillus Fumigatus Phosphomannomutase


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 Aspergillus Fumigatus Phosphomannomutase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg301

b:13.7
occ:1.00
 OD1 B:ASP226 1.9 14.4 1.0
O B:HOH472 2.0 12.2 1.0
O B:ASP22 2.1 21.5 1.0
O B:HOH427 2.1 9.6 1.0
OD2 B:ASP20 2.1 12.6 1.0
O B:HOH530 2.2 15.8 1.0
CG B:ASP226 3.0 14.6 1.0
CG B:ASP20 3.0 13.4 1.0
C B:ASP22 3.2 21.9 1.0
OD1 B:ASP20 3.3 11.9 1.0
OD2 B:ASP226 3.4 15.5 1.0
CA B:ASP22 3.9 22.4 1.0
OG1 B:THR24 4.0 14.8 1.0
N B:ASP22 4.0 20.3 1.0
OD2 B:ASP234 4.1 12.0 1.0
CB B:ASP22 4.1 28.6 1.0
CB B:ASP226 4.3 14.1 1.0
N B:GLU23 4.3 21.4 1.0
CB B:ASP20 4.3 12.7 1.0
CB B:GLU23 4.4 23.6 1.0
N B:ASP226 4.5 12.6 1.0
O B:HOH466 4.5 29.0 1.0
CA B:GLU23 4.6 20.9 1.0
C B:GLU23 4.6 21.2 1.0
CG B:LYS227 4.6 18.4 1.0
N B:THR24 4.7 19.4 1.0
C B:VAL21 4.8 17.3 1.0
CA B:ASP226 4.9 13.5 1.0
CB B:THR24 4.9 16.2 1.0
O B:HOH534 4.9 24.0 1.0
CG B:ASP234 5.0 13.7 1.0
OD1 B:ASN233 5.0 38.9 1.0

Magnesium binding site 3 out of 4 in 6i5x

Go back to Magnesium Binding Sites List in 6i5x
Magnesium binding site 3 out of 4 in the Crystal Structure of Aspergillus Fumigatus Phosphomannomutase


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 Aspergillus Fumigatus Phosphomannomutase within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg301

b:22.0
occ:1.00
 O C:HOH420 1.8 16.6 1.0
O C:HOH426 1.9 11.2 1.0
O C:HOH470 1.9 14.4 1.0
OD2 C:ASP20 2.1 14.0 1.0
O C:ASP22 2.1 16.8 1.0
OD1 C:ASP226 2.1 20.1 1.0
CG C:ASP20 3.0 13.7 1.0
CG C:ASP226 3.1 19.0 1.0
C C:ASP22 3.2 18.2 1.0
OD1 C:ASP20 3.3 14.6 1.0
OD2 C:ASP226 3.5 20.3 1.0
CA C:ASP22 3.9 19.8 1.0
N C:ASP22 4.1 17.6 1.0
CB C:ASP22 4.1 21.9 1.0
OD2 C:ASP234 4.1 14.0 1.0
OG1 C:THR24 4.2 15.2 1.0
N C:GLU23 4.3 19.9 1.0
CB C:ASP20 4.4 13.1 1.0
CB C:GLU23 4.4 26.9 1.0
CB C:ASP226 4.5 16.8 1.0
N C:ASP226 4.6 14.1 1.0
CG C:LYS227 4.7 20.0 1.0
CA C:GLU23 4.7 22.7 1.0
C C:GLU23 4.7 19.0 1.0
C C:VAL21 4.8 16.0 1.0
N C:THR24 4.8 17.6 1.0
O C:HOH576 5.0 29.1 1.0

Magnesium binding site 4 out of 4 in 6i5x

Go back to Magnesium Binding Sites List in 6i5x
Magnesium binding site 4 out of 4 in the Crystal Structure of Aspergillus Fumigatus Phosphomannomutase


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 Aspergillus Fumigatus Phosphomannomutase within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg301

b:14.2
occ:1.00
 O D:ASP22 1.9 17.8 1.0
O D:HOH462 2.0 8.9 1.0
OD1 D:ASP226 2.0 13.4 1.0
O D:HOH433 2.1 11.8 1.0
O D:HOH440 2.2 14.0 1.0
OD2 D:ASP20 2.3 12.3 1.0
C D:ASP22 3.0 18.3 1.0
CG D:ASP226 3.0 14.8 1.0
CG D:ASP20 3.1 12.6 1.0
OD2 D:ASP226 3.4 14.3 1.0
OD1 D:ASP20 3.4 10.9 1.0
CA D:ASP22 3.8 19.9 1.0
N D:ASP22 4.0 17.4 1.0
CB D:ASP22 4.1 25.8 1.0
N D:GLU23 4.1 16.6 1.0
OG1 D:THR24 4.2 12.6 1.0
OD2 D:ASP234 4.2 14.3 1.0
CB D:GLU23 4.4 18.8 1.0
CB D:ASP226 4.4 15.0 1.0
O D:HOH412 4.5 25.9 1.0
CB D:ASP20 4.5 12.0 1.0
CG D:LYS227 4.6 20.1 1.0
CA D:GLU23 4.6 17.6 1.0
N D:ASP226 4.6 13.0 1.0
C D:GLU23 4.7 17.1 1.0
C D:VAL21 4.7 15.8 1.0
N D:THR24 4.8 17.3 1.0
O D:HOH577 4.9 23.4 1.0
CA D:ASP226 5.0 14.7 1.0
CB D:THR24 5.0 15.2 1.0

Reference:

Y.Zhang, O.G.Raimi, A.T.Ferenbach, D.M.F.Van Aalten. Crystal Structure of Aspergillus Fumigatus Phosphomannomutase To Be Published.
Page generated: Mon Dec 14 22:56:20 2020

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