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Manganese in PDB 3v8z: Structure of Apo-Glycogenin Truncated at Residue 270 Complexed with Udp

Enzymatic activity of Structure of Apo-Glycogenin Truncated at Residue 270 Complexed with Udp

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

Protein crystallography data

The structure of Structure of Apo-Glycogenin Truncated at Residue 270 Complexed with Udp, PDB code: 3v8z 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) 25.74 / 2.20
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 56.940, 105.170, 120.540, 90.00, 90.00, 90.00
R / Rfree (%) 19.9 / 23.8

Other elements in 3v8z:

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

Chlorine (Cl) 1 atom

Manganese Binding Sites:

The binding sites of Manganese atom in the Structure of Apo-Glycogenin Truncated at Residue 270 Complexed with Udp (pdb code 3v8z). 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 Apo-Glycogenin Truncated at Residue 270 Complexed with Udp, PDB code: 3v8z:

Manganese binding site 1 out of 1 in 3v8z

Go back to Manganese Binding Sites List in 3v8z
Manganese binding site 1 out of 1 in the Structure of Apo-Glycogenin Truncated at Residue 270 Complexed with Udp


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of Apo-Glycogenin Truncated at Residue 270 Complexed with Udp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn304

b:23.3
occ:1.00
 OD2 A:ASP101 2.1 13.8 1.0
NE2 A:HIS211 2.1 14.3 1.0
OD1 A:ASP103 2.2 16.9 1.0
O2B A:UDP305 2.2 29.9 1.0
O2A A:UDP305 2.4 30.9 1.0
OD2 A:ASP103 2.5 19.6 1.0
CG A:ASP103 2.7 16.4 1.0
CG A:ASP101 3.0 11.3 1.0
CE1 A:HIS211 3.0 13.7 1.0
O5' A:UDP305 3.1 35.0 1.0
CD2 A:HIS211 3.1 13.9 1.0
PA A:UDP305 3.1 31.2 1.0
CB A:ASP101 3.3 10.9 1.0
PB A:UDP305 3.4 29.2 1.0
O3' A:UDP305 3.6 29.9 1.0
O3A A:UDP305 3.6 31.7 1.0
O1B A:UDP305 3.9 30.4 1.0
CB A:ASP103 4.2 13.6 1.0
CD2 A:LEU213 4.2 30.1 1.0
ND1 A:HIS211 4.2 13.9 1.0
O A:HOH477 4.2 19.9 1.0
OD1 A:ASP101 4.2 10.2 1.0
NZ A:LYS217 4.2 19.5 1.0
CG A:HIS211 4.2 14.6 1.0
C5' A:UDP305 4.4 32.3 1.0
C3' A:UDP305 4.5 30.1 1.0
O1A A:UDP305 4.5 33.5 1.0
O3B A:UDP305 4.6 30.3 1.0
C4' A:UDP305 4.7 30.8 1.0
O A:HOH413 4.7 41.9 1.0
CA A:ASP101 4.8 10.8 1.0
N A:ASP103 4.9 12.3 1.0
CA A:ASP103 4.9 13.5 1.0
O A:PHE212 5.0 22.7 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 18:20:16 2024

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