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Manganese in PDB 1ll2: Crystal Structure of Rabbit Muscle Glycogenin Complexed with Udp- Glucose and Manganese

Enzymatic activity of Crystal Structure of Rabbit Muscle Glycogenin Complexed with Udp- Glucose and Manganese

All present enzymatic activity of Crystal Structure of Rabbit Muscle Glycogenin Complexed with Udp- Glucose and Manganese:
2.4.1.186;

Protein crystallography data

The structure of Crystal Structure of Rabbit Muscle Glycogenin Complexed with Udp- Glucose and Manganese, PDB code: 1ll2 was solved by B.J.Gibbons, P.J.Roach, T.D.Hurley, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.90
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 57.887, 106.875, 122.253, 90.00, 90.00, 90.00
R / Rfree (%) 19.4 / 22.7

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Rabbit Muscle Glycogenin Complexed with Udp- Glucose and Manganese (pdb code 1ll2). 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 Rabbit Muscle Glycogenin Complexed with Udp- Glucose and Manganese, PDB code: 1ll2:

Manganese binding site 1 out of 1 in 1ll2

Go back to Manganese Binding Sites List in 1ll2
Manganese binding site 1 out of 1 in the Crystal Structure of Rabbit Muscle Glycogenin Complexed with Udp- Glucose and Manganese


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 Rabbit Muscle Glycogenin Complexed with Udp- Glucose and Manganese within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn333

b:26.0
occ:1.00
OD2 A:ASP102 2.1 25.7 1.0
O1B A:UPG334 2.1 27.2 1.0
OD1 A:ASP104 2.2 24.1 1.0
NE2 A:HIS212 2.2 21.7 1.0
O1A A:UPG334 2.3 27.4 1.0
OD2 A:ASP104 2.6 26.0 1.0
CG A:ASP104 2.7 25.4 1.0
CG A:ASP102 3.1 24.4 1.0
CE1 A:HIS212 3.2 24.3 1.0
CD2 A:HIS212 3.2 24.8 1.0
PB A:UPG334 3.4 29.7 1.0
PA A:UPG334 3.5 30.2 1.0
CB A:ASP102 3.5 24.1 1.0
O3A A:UPG334 3.6 29.9 1.0
O3C A:UPG334 3.8 29.8 1.0
O2B A:UPG334 4.0 30.5 1.0
C5C A:UPG334 4.1 27.7 1.0
O5C A:UPG334 4.2 27.4 1.0
CB A:ASP104 4.2 23.6 1.0
OD1 A:ASP102 4.2 23.9 1.0
ND1 A:HIS212 4.3 22.8 1.0
CG A:HIS212 4.4 22.7 1.0
NZ A:LYS218 4.4 27.2 1.0
C3C A:UPG334 4.5 27.1 1.0
O3B A:UPG334 4.5 33.8 1.0
C4C A:UPG334 4.7 27.6 1.0
O2A A:UPG334 4.7 30.7 1.0
CA A:LEU214 4.7 38.0 1.0
O5' A:UPG334 4.8 38.9 1.0
C6' A:UPG334 4.8 42.7 1.0
O6' A:UPG334 4.8 45.8 1.0
C5' A:UPG334 4.8 42.1 1.0
N A:ASP104 4.9 23.2 1.0
CA A:ASP102 4.9 25.3 1.0
CA A:ASP104 5.0 23.9 1.0

Reference:

B.J.Gibbons, P.J.Roach, T.D.Hurley. Crystal Structure of the Autocatalytic Initiator of Glycogen Biosynthesis, Glycogenin. J.Mol.Biol. V. 319 463 2002.
ISSN: ISSN 0022-2836
PubMed: 12051921
DOI: 10.1016/S0022-2836(02)00305-4
Page generated: Sat Oct 5 11:29:57 2024

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