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Manganese in PDB 3rmv: Crystal Structure of Human Glycogenin-1 (GYG1) T83M Mutant Complexed with Manganese and Udp

Enzymatic activity of Crystal Structure of Human Glycogenin-1 (GYG1) T83M Mutant Complexed with Manganese and Udp

All present enzymatic activity of Crystal Structure of Human Glycogenin-1 (GYG1) T83M Mutant Complexed with Manganese and Udp:
2.4.1.186;

Protein crystallography data

The structure of Crystal Structure of Human Glycogenin-1 (GYG1) T83M Mutant Complexed with Manganese and Udp, PDB code: 3rmv was solved by A.Chaikuad, D.S.Froese, W.W.Yue, E.Krysztofinska, F.Von Delft, J.Weigelt, C.H.Arrowsmith, A.M.Edwards, C.Bountra, U.Oppermann, Structural Genomicsconsortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.34 / 1.82
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 56.680, 100.720, 48.720, 90.00, 90.00, 90.00
R / Rfree (%) 18.3 / 22.6

Other elements in 3rmv:

The structure of Crystal Structure of Human Glycogenin-1 (GYG1) T83M Mutant Complexed with Manganese and Udp also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Human Glycogenin-1 (GYG1) T83M Mutant Complexed with Manganese and Udp (pdb code 3rmv). 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 Crystal Structure of Human Glycogenin-1 (GYG1) T83M Mutant Complexed with Manganese and Udp, PDB code: 3rmv:

Manganese binding site 1 out of 1 in 3rmv

Go back to Manganese Binding Sites List in 3rmv
Manganese binding site 1 out of 1 in the Crystal Structure of Human Glycogenin-1 (GYG1) T83M Mutant Complexed with Manganese and Udp


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Human Glycogenin-1 (GYG1) T83M Mutant Complexed with Manganese and Udp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn263

b:17.4
occ:1.00
 OD2 A:ASP102 2.0 18.7 1.0
O1A A:UDP264 2.0 19.6 1.0
O3B A:UDP264 2.0 18.5 1.0
OD1 A:ASP104 2.0 21.1 1.0
NE2 A:HIS212 2.1 17.6 1.0
OD2 A:ASP104 2.5 18.6 1.0
CG A:ASP104 2.6 17.4 1.0
CG A:ASP102 3.0 19.7 1.0
CE1 A:HIS212 3.1 15.7 1.0
CD2 A:HIS212 3.1 14.2 1.0
PB A:UDP264 3.3 24.4 1.0
PA A:UDP264 3.4 21.8 1.0
CB A:ASP102 3.5 19.7 1.0
O3A A:UDP264 3.6 21.2 1.0
O3' A:UDP264 3.9 19.2 1.0
O2B A:UDP264 4.0 20.5 1.0
O A:HOH424 4.1 29.5 1.0
OD1 A:ASP102 4.1 19.1 1.0
CB A:ASP104 4.2 15.3 1.0
C5' A:UDP264 4.2 19.9 1.0
O A:HOH423 4.2 35.3 1.0
ND1 A:HIS212 4.2 19.6 1.0
CG A:HIS212 4.3 20.0 1.0
NZ A:LYS218 4.3 16.6 1.0
O5' A:UDP264 4.3 22.2 1.0
O2A A:UDP264 4.5 21.9 1.0
O1B A:UDP264 4.5 23.6 1.0
CA A:LEU214 4.6 29.3 1.0
C3' A:UDP264 4.7 22.5 1.0
C4' A:UDP264 4.8 20.6 1.0
CA A:ASP102 5.0 19.0 1.0
CB A:LEU214 5.0 28.1 1.0
N A:LEU214 5.0 28.8 1.0
N A:ASP104 5.0 16.5 1.0
CA A:ASP104 5.0 15.0 1.0

Reference:

A.Chaikuad, D.S.Froese, G.Berridge, F.Von Delft, U.Oppermann, W.W.Yue. Conformational Plasticity of Glycogenin and Its Maltosaccharide Substrate During Glycogen Biogenesis. Proc.Natl.Acad.Sci.Usa V. 108 21028 2011.
ISSN: ISSN 0027-8424
PubMed: 22160680
DOI: 10.1073/PNAS.1113921108
Page generated: Sat Oct 5 17:50:06 2024

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