Iodine in PDB 6eql: Crystal Structure of Human Glycogenin-1 (GYG1) TYR195PIPHE Mutant Complexed with Manganese and Udp

Enzymatic activity of Crystal Structure of Human Glycogenin-1 (GYG1) TYR195PIPHE Mutant Complexed with Manganese and Udp

All present enzymatic activity of Crystal Structure of Human Glycogenin-1 (GYG1) TYR195PIPHE Mutant Complexed with Manganese and Udp:
2.4.1.186;

Protein crystallography data

The structure of Crystal Structure of Human Glycogenin-1 (GYG1) TYR195PIPHE Mutant Complexed with Manganese and Udp, PDB code: 6eql was solved by H.J.Bailey, J.Kopec, M.K.Bilyard, G.A.Bezerra, S.Seo Lee, C.H.Arrowsmith, A.M.Edwards, C.Bountra, B.G.Davis, W.W.Yue, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.55 / 2.38
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 66.170, 81.050, 111.200, 90.00, 90.00, 90.00
R / Rfree (%) 22.5 / 28.1

Other elements in 6eql:

The structure of Crystal Structure of Human Glycogenin-1 (GYG1) TYR195PIPHE Mutant Complexed with Manganese and Udp also contains other interesting chemical elements:

Manganese (Mn) 2 atoms

Iodine Binding Sites:

The binding sites of Iodine atom in the Crystal Structure of Human Glycogenin-1 (GYG1) TYR195PIPHE Mutant Complexed with Manganese and Udp (pdb code 6eql). This binding sites where shown within 5.0 Angstroms radius around Iodine atom.
In total only one binding site of Iodine was determined in the Crystal Structure of Human Glycogenin-1 (GYG1) TYR195PIPHE Mutant Complexed with Manganese and Udp, PDB code: 6eql:

Iodine binding site 1 out of 1 in 6eql

Go back to Iodine Binding Sites List in 6eql
Iodine binding site 1 out of 1 in the Crystal Structure of Human Glycogenin-1 (GYG1) TYR195PIPHE Mutant Complexed with Manganese and Udp


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 1 of Crystal Structure of Human Glycogenin-1 (GYG1) TYR195PIPHE Mutant Complexed with Manganese and Udp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:I195

b:66.8
occ:0.65
 I A:PHI195 0.0 66.8 0.7
CZ A:PHI195 2.0 63.6 0.7
CE2 A:PHI195 3.0 49.7 0.7
CE1 A:PHI195 3.0 52.4 0.7
O A:PRO126 3.8 49.3 1.0
N B:GLY127 4.1 43.2 1.0
CA A:GLY127 4.2 52.8 1.0
CD2 A:PHI195 4.3 50.2 0.7
CD1 A:PHI195 4.3 51.5 0.7
C A:PRO126 4.3 43.8 1.0
CG2 A:ILE194 4.4 65.2 1.0
CA B:GLY127 4.4 41.1 1.0
N A:GLY127 4.5 49.6 1.0
CB B:PRO126 4.7 39.3 1.0
C B:PRO126 4.8 43.5 1.0
CG A:PHI195 4.8 50.9 0.7
CB A:PRO126 4.9 42.0 1.0

Reference:

M.K.Bilyard, H.J.Bailey, L.Raich, M.A.Gafitescu, T.Machida, J.Iglesias-Fernandez, S.S.Lee, C.D.Spicer, C.Rovira, W.W.Yue, B.G.Davis. Palladium-Mediated Enzyme Activation Suggests Multiphase Initiation of Glycogenesis. Nature V. 563 235 2018.
ISSN: ESSN 1476-4687
PubMed: 30356213
DOI: 10.1038/S41586-018-0644-7
Page generated: Sun Dec 13 19:43:46 2020

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