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Manganese in PDB 2ify: Structure of Bacillus Anthracis Cofactor-Independent Phosphoglucerate Mutase

Enzymatic activity of Structure of Bacillus Anthracis Cofactor-Independent Phosphoglucerate Mutase

All present enzymatic activity of Structure of Bacillus Anthracis Cofactor-Independent Phosphoglucerate Mutase:
5.4.2.1;

Protein crystallography data

The structure of Structure of Bacillus Anthracis Cofactor-Independent Phosphoglucerate Mutase, PDB code: 2ify was solved by M.Nukui, J.E.Littlejohn, M.J.Jedrzejas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.41 / 2.38
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 43.620, 72.737, 185.176, 90.00, 90.00, 90.00
R / Rfree (%) 24.5 / 29.8

Manganese Binding Sites:

The binding sites of Manganese atom in the Structure of Bacillus Anthracis Cofactor-Independent Phosphoglucerate Mutase (pdb code 2ify). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Structure of Bacillus Anthracis Cofactor-Independent Phosphoglucerate Mutase, PDB code: 2ify:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 2ify

Go back to Manganese Binding Sites List in 2ify
Manganese binding site 1 out of 2 in the Structure of Bacillus Anthracis Cofactor-Independent Phosphoglucerate Mutase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of Bacillus Anthracis Cofactor-Independent Phosphoglucerate Mutase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn601

b:32.1
occ:1.00
NE2 A:HIS461 2.2 50.2 1.0
OD2 A:ASP402 2.3 52.6 1.0
NE2 A:HIS406 2.4 50.5 1.0
O A:HOH716 2.9 24.7 1.0
OD1 A:ASP402 3.0 43.3 1.0
CG A:ASP402 3.0 50.9 1.0
CE1 A:HIS461 3.1 50.2 1.0
CD2 A:HIS461 3.2 51.8 1.0
CE1 A:HIS406 3.4 49.9 1.0
CD2 A:HIS406 3.4 49.9 1.0
OG A:SER61 4.0 48.8 1.0
NZ A:LYS335 4.1 46.2 1.0
ND1 A:HIS461 4.2 49.5 1.0
CG A:HIS461 4.3 51.7 1.0
CE1 A:HIS444 4.4 50.2 1.0
CB A:ASP402 4.5 51.6 1.0
ND1 A:HIS406 4.5 50.0 1.0
NE2 A:HIS444 4.5 50.6 1.0
O A:HOH819 4.5 28.6 1.0
CG A:HIS406 4.5 51.1 1.0
OD1 A:ASN446 4.7 51.2 1.0
O A:ASP402 4.8 53.0 1.0
MN A:MN701 5.0 29.9 1.0

Manganese binding site 2 out of 2 in 2ify

Go back to Manganese Binding Sites List in 2ify
Manganese binding site 2 out of 2 in the Structure of Bacillus Anthracis Cofactor-Independent Phosphoglucerate Mutase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Structure of Bacillus Anthracis Cofactor-Independent Phosphoglucerate Mutase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn701

b:29.9
occ:1.00
OD2 A:ASP443 2.2 45.8 1.0
OD1 A:ASP11 2.3 49.1 1.0
NE2 A:HIS444 2.3 50.6 1.0
OG A:SER61 2.5 48.8 1.0
CD2 A:HIS444 2.9 50.5 1.0
CG A:ASP11 2.9 48.9 1.0
OD2 A:ASP11 2.9 45.3 1.0
CG A:ASP443 2.9 49.5 1.0
OD1 A:ASP443 2.9 49.5 1.0
CB A:SER61 3.0 51.0 1.0
CA A:SER61 3.1 51.5 1.0
CE1 A:HIS444 3.5 50.2 1.0
N A:SER61 3.6 52.0 1.0
NZ A:LYS335 3.8 46.2 1.0
CG A:HIS444 4.1 50.5 1.0
CG A:ASP402 4.1 50.9 1.0
OD2 A:ASP402 4.1 52.6 1.0
OD1 A:ASP402 4.3 43.3 1.0
CB A:ASP11 4.3 48.2 1.0
ND1 A:HIS444 4.4 49.8 1.0
C A:ASN60 4.4 52.2 1.0
CB A:ASP443 4.4 49.8 1.0
NE2 A:HIS65 4.5 48.0 1.0
C A:SER61 4.5 51.5 1.0
CE A:LYS335 4.6 47.7 1.0
CA A:ASP11 4.6 48.7 1.0
CB A:ASP402 4.7 51.6 1.0
N A:GLY12 4.7 47.4 1.0
CD2 A:HIS65 4.7 46.0 1.0
O A:ASN60 4.8 52.5 1.0
O A:SER61 4.8 52.4 1.0
C A:ASP11 4.9 48.4 1.0
CD A:LYS335 4.9 47.2 1.0
MN A:MN601 5.0 32.1 1.0

Reference:

M.Nukui, L.V.Mello, J.E.Littlejohn, B.Setlow, P.Setlow, K.Kim, T.Leighton, M.J.Jedrzejas. Structure and Molecular Mechanism of Bacillus Anthracis Cofactor-Independent Phosphoglycerate Mutase: A Crucial Enzyme For Spores and Growing Cells of Bacillus Species. Biophys.J. V. 92 977 2007.
ISSN: ISSN 0006-3495
PubMed: 17085493
DOI: 10.1529/BIOPHYSJ.106.093872
Page generated: Sat Oct 5 14:28:24 2024

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