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Manganese in PDB 3tx0: Unphosphorylated Bacillus Cereus Phosphopentomutase in A P212121 Crystal Form

Enzymatic activity of Unphosphorylated Bacillus Cereus Phosphopentomutase in A P212121 Crystal Form

All present enzymatic activity of Unphosphorylated Bacillus Cereus Phosphopentomutase in A P212121 Crystal Form:
5.4.2.7;

Protein crystallography data

The structure of Unphosphorylated Bacillus Cereus Phosphopentomutase in A P212121 Crystal Form, PDB code: 3tx0 was solved by T.P.Panosian, D.P.Nanneman, B.O.Bachmann, T.M.Iverson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.26
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 60.975, 75.706, 95.562, 90.00, 90.00, 90.00
R / Rfree (%) 18.9 / 24.6

Manganese Binding Sites:

The binding sites of Manganese atom in the Unphosphorylated Bacillus Cereus Phosphopentomutase in A P212121 Crystal Form (pdb code 3tx0). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Unphosphorylated Bacillus Cereus Phosphopentomutase in A P212121 Crystal Form, PDB code: 3tx0:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 3tx0

Go back to Manganese Binding Sites List in 3tx0
Manganese binding site 1 out of 2 in the Unphosphorylated Bacillus Cereus Phosphopentomutase in A P212121 Crystal Form


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Unphosphorylated Bacillus Cereus Phosphopentomutase in A P212121 Crystal Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn395

b:44.3
occ:1.00
NE2 A:HIS339 1.9 30.9 1.0
OD1 A:ASP286 1.9 30.8 1.0
OD2 A:ASP156 2.1 35.5 1.0
NE2 A:HIS291 2.2 32.9 1.0
CG A:ASP286 2.8 29.8 1.0
CD2 A:HIS339 2.8 29.8 1.0
CG A:ASP156 2.9 39.8 1.0
CE1 A:HIS339 2.9 30.9 1.0
OD1 A:ASP156 3.0 44.6 1.0
OD2 A:ASP286 3.0 30.1 1.0
CD2 A:HIS291 3.1 33.4 1.0
CE1 A:HIS291 3.2 31.3 1.0
O A:ALA155 3.9 37.4 1.0
CG A:HIS339 4.0 29.2 1.0
ND1 A:HIS339 4.0 28.3 1.0
CB A:ASP286 4.2 26.8 1.0
CG A:HIS291 4.2 31.8 1.0
ND1 A:HIS291 4.3 33.2 1.0
CG2 A:VAL103 4.3 20.9 1.0
CB A:ASP156 4.3 38.1 1.0
OG1 A:THR85 4.4 27.2 1.0
CE1 A:HIS328 4.4 26.0 1.0
C A:ALA155 4.4 37.6 1.0
ND2 A:ASN330 4.4 25.0 1.0
CB A:ALA155 4.6 37.0 1.0
NE2 A:HIS328 4.7 24.3 1.0
CA A:ASP156 4.8 37.6 1.0
N A:ASP156 4.8 37.6 1.0
MN A:MN396 5.0 63.9 1.0

Manganese binding site 2 out of 2 in 3tx0

Go back to Manganese Binding Sites List in 3tx0
Manganese binding site 2 out of 2 in the Unphosphorylated Bacillus Cereus Phosphopentomutase in A P212121 Crystal Form


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Unphosphorylated Bacillus Cereus Phosphopentomutase in A P212121 Crystal Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn396

b:63.9
occ:1.00
OG1 A:THR85 2.1 27.2 1.0
NE2 A:HIS328 2.1 24.3 1.0
OD1 A:ASP13 2.1 27.8 1.0
OD2 A:ASP327 2.4 27.6 1.0
CG A:ASP13 2.8 28.0 1.0
CD2 A:HIS328 2.9 23.6 1.0
OD2 A:ASP13 3.0 30.6 1.0
CB A:THR85 3.0 25.0 1.0
CG A:ASP327 3.1 26.7 1.0
OD1 A:ASP327 3.2 27.9 1.0
CE1 A:HIS328 3.2 26.0 1.0
CG2 A:THR85 3.4 24.0 1.0
CA A:THR85 3.4 24.9 1.0
OD1 A:ASP156 4.0 44.6 1.0
CG A:HIS328 4.1 22.7 1.0
N A:THR85 4.1 24.7 1.0
CB A:ASP13 4.2 25.0 1.0
ND1 A:HIS328 4.2 23.4 1.0
N A:SER14 4.4 22.5 1.0
CE1 A:HIS339 4.4 30.9 1.0
NE2 A:HIS89 4.5 16.4 1.0
OD1 A:ASP286 4.5 30.8 1.0
CA A:ASP13 4.5 24.7 1.0
CB A:ASP327 4.6 25.0 1.0
CG A:ASP286 4.7 29.8 1.0
C A:THR85 4.7 25.5 1.0
C A:ASP13 4.8 24.0 1.0
NE2 A:HIS339 4.8 30.9 1.0
CD2 A:HIS89 4.8 16.1 1.0
C A:ASP84 4.9 24.0 1.0
O A:THR85 4.9 25.8 1.0
CB A:ASP286 4.9 26.8 1.0
MN A:MN395 5.0 44.3 1.0
ND1 A:HIS339 5.0 28.3 1.0

Reference:

T.M.Iverson, T.D.Panosian, W.R.Birmingham, D.P.Nannemann, B.O.Bachmann. Molecular Differences Between A Mutase and A Phosphatase: Investigations of the Activation Step in Bacillus Cereus Phosphopentomutase. Biochemistry V. 51 1964 2012.
ISSN: ISSN 0006-2960
PubMed: 22329805
DOI: 10.1021/BI201761H
Page generated: Sat Oct 5 18:02:15 2024

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