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Manganese in PDB 6tex: Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - VAL80LYS Mutant - Cocrystal with FE2+, MN2+, Udp-Glucose

Enzymatic activity of Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - VAL80LYS Mutant - Cocrystal with FE2+, MN2+, Udp-Glucose

All present enzymatic activity of Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - VAL80LYS Mutant - Cocrystal with FE2+, MN2+, Udp-Glucose:
1.14.11.4; 2.4.1.50; 2.4.1.66;

Protein crystallography data

The structure of Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - VAL80LYS Mutant - Cocrystal with FE2+, MN2+, Udp-Glucose, PDB code: 6tex was solved by A.Chiapparino, F.De Giorgi, L.Scietti, S.Faravelli, T.Roscioli, F.Forneris, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.00 / 2.30
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 98.049, 100.409, 225.179, 90, 90, 90
R / Rfree (%) 17 / 22.6

Other elements in 6tex:

The structure of Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - VAL80LYS Mutant - Cocrystal with FE2+, MN2+, Udp-Glucose also contains other interesting chemical elements:

Iron (Fe) 2 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - VAL80LYS Mutant - Cocrystal with FE2+, MN2+, Udp-Glucose (pdb code 6tex). 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 Full-Length Human Lysyl Hydroxylase LH3 - VAL80LYS Mutant - Cocrystal with FE2+, MN2+, Udp-Glucose, PDB code: 6tex:

Manganese binding site 1 out of 1 in 6tex

Go back to Manganese Binding Sites List in 6tex
Manganese binding site 1 out of 1 in the Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - VAL80LYS Mutant - Cocrystal with FE2+, MN2+, Udp-Glucose


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 Full-Length Human Lysyl Hydroxylase LH3 - VAL80LYS Mutant - Cocrystal with FE2+, MN2+, Udp-Glucose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn807

b:31.7
occ:1.00
 O3B A:UDP804 2.0 34.4 1.0
O1A A:UDP804 2.1 38.6 1.0
OD2 A:ASP112 2.2 30.0 1.0
OD2 A:ASP115 2.2 33.7 1.0
NE2 A:HIS253 2.3 23.5 1.0
OD1 A:ASP115 2.4 27.9 1.0
CG A:ASP115 2.6 31.7 1.0
CG A:ASP112 3.1 32.3 1.0
CD2 A:HIS253 3.2 28.8 1.0
CE1 A:HIS253 3.3 34.1 1.0
PB A:UDP804 3.4 31.5 1.0
PA A:UDP804 3.4 32.4 1.0
CB A:ASP112 3.5 25.8 1.0
O3A A:UDP804 3.6 36.6 1.0
O3' A:UDP804 3.9 41.3 1.0
O2B A:UDP804 4.0 37.6 1.0
CB A:ASP115 4.2 29.6 1.0
OD1 A:ASP112 4.3 30.0 1.0
C5' A:UDP804 4.3 39.0 1.0
O5' A:UDP804 4.3 30.1 1.0
ND1 A:HIS253 4.4 28.8 1.0
CG A:HIS253 4.4 29.8 1.0
O2A A:UDP804 4.4 42.5 1.0
CA A:ASN255 4.5 35.5 1.0
O1B A:UDP804 4.6 43.4 1.0
NZ A:LYS259 4.7 39.3 1.0
C4' A:UDP804 4.7 35.0 1.0
C3' A:UDP804 4.8 38.7 1.0
CB A:ASN255 4.8 32.6 1.0
O A:ASP115 5.0 32.9 1.0
O A:GLY254 5.0 30.9 1.0

Reference:

A.Chiapparino, F.De Giorgi, L.Scietti, S.Faravelli, T.Roscioli, F.Forneris. A Cooperative Network of Molecular "Hot Spots" Highlights the Complexity of LH3 Collagen Glycosyltransferase Activities To Be Published.
Page generated: Sun Oct 6 07:11:29 2024

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