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Manganese in PDB 3v91: Structure of T82M Glycogenin Mutant Truncated at Residue 270 Complexed with Udp-Glucose

Enzymatic activity of Structure of T82M Glycogenin Mutant Truncated at Residue 270 Complexed with Udp-Glucose

All present enzymatic activity of Structure of T82M Glycogenin Mutant Truncated at Residue 270 Complexed with Udp-Glucose:
2.4.1.186;

Protein crystallography data

The structure of Structure of T82M Glycogenin Mutant Truncated at Residue 270 Complexed with Udp-Glucose, PDB code: 3v91 was solved by M.E.Carrizo, J.M.Romero, F.M.Issoglio, J.A.Curtino, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.37 / 2.00
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 58.210, 103.510, 119.870, 90.00, 90.00, 90.00
R / Rfree (%) 20.6 / 23.6

Other elements in 3v91:

The structure of Structure of T82M Glycogenin Mutant Truncated at Residue 270 Complexed with Udp-Glucose also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Manganese Binding Sites:

The binding sites of Manganese atom in the Structure of T82M Glycogenin Mutant Truncated at Residue 270 Complexed with Udp-Glucose (pdb code 3v91). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Structure of T82M Glycogenin Mutant Truncated at Residue 270 Complexed with Udp-Glucose, PDB code: 3v91:

Manganese binding site 1 out of 1 in 3v91

Go back to Manganese Binding Sites List in 3v91
Manganese binding site 1 out of 1 in the Structure of T82M Glycogenin Mutant Truncated at Residue 270 Complexed with Udp-Glucose


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of T82M Glycogenin Mutant Truncated at Residue 270 Complexed with Udp-Glucose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn303

b:32.9
occ:1.00
 NE2 A:HIS211 2.1 20.8 1.0
OD1 A:ASP103 2.2 25.1 1.0
O1B A:UPG304 2.2 45.5 1.0
OD2 A:ASP101 2.2 25.9 1.0
O1A A:UPG304 2.4 44.4 1.0
OD2 A:ASP103 2.5 30.6 1.0
CG A:ASP103 2.7 25.1 1.0
CD2 A:HIS211 3.0 19.6 1.0
CG A:ASP101 3.1 21.7 1.0
CE1 A:HIS211 3.2 20.9 1.0
CB A:ASP101 3.3 20.8 1.0
PB A:UPG304 3.4 45.7 1.0
PA A:UPG304 3.6 44.3 1.0
O3C A:UPG304 3.6 39.5 1.0
O3A A:UPG304 3.7 45.5 1.0
C5C A:UPG304 4.1 42.0 1.0
CB A:ASP103 4.2 22.4 1.0
CG A:HIS211 4.2 21.3 1.0
O2B A:UPG304 4.3 45.1 1.0
ND1 A:HIS211 4.3 20.9 1.0
OD1 A:ASP101 4.3 22.6 1.0
O5C A:UPG304 4.4 44.5 1.0
NZ A:LYS217 4.4 33.9 1.0
C3C A:UPG304 4.5 39.3 1.0
C6' A:UPG304 4.5 44.1 1.0
O5' A:UPG304 4.5 45.8 1.0
C5' A:UPG304 4.5 46.0 1.0
C4C A:UPG304 4.6 40.4 1.0
O3B A:UPG304 4.6 46.1 1.0
O6' A:UPG304 4.7 42.5 1.0
O2A A:UPG304 4.8 45.7 1.0
CA A:ASP101 4.8 20.5 1.0
N A:ASP103 4.9 21.1 1.0
CA A:ASP103 4.9 21.9 1.0
O A:PHE212 4.9 32.7 1.0
C A:ASP103 5.0 21.4 1.0

Reference:

M.E.Carrizo, J.M.Romero, F.M.Issoglio, J.A.Curtino. Structural and Biochemical Insight Into Glycogenin Inactivation By the Glycogenosis-Causing T82M Mutation. Febs Lett. V. 586 254 2012.
ISSN: ISSN 0014-5793
PubMed: 22226635
DOI: 10.1016/J.FEBSLET.2011.12.028
Page generated: Sat Oct 5 18:20:39 2024

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