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Manganese in PDB 6tec: Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - Cocrystal with FE2+, MN2+, Udp-Xylose

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

All present enzymatic activity of Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - Cocrystal with FE2+, MN2+, Udp-Xylose:
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 - Cocrystal with FE2+, MN2+, Udp-Xylose, PDB code: 6tec 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) 48.79 / 2.40
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 97.264, 99.987, 223.96, 90, 90, 90
R / Rfree (%) 18.5 / 21.6

Other elements in 6tec:

The structure of Crystal Structure of Full-Length Human Lysyl Hydroxylase LH3 - Cocrystal with FE2+, MN2+, Udp-Xylose 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 - Cocrystal with FE2+, MN2+, Udp-Xylose (pdb code 6tec). 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 - Cocrystal with FE2+, MN2+, Udp-Xylose, PDB code: 6tec:

Manganese binding site 1 out of 1 in 6tec

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


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 - Cocrystal with FE2+, MN2+, Udp-Xylose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn805

b:30.6
occ:1.00
 O1B A:UDX801 1.9 36.6 1.0
NE2 A:HIS253 2.3 15.7 1.0
OD2 A:ASP112 2.3 28.3 1.0
OD1 A:ASP115 2.3 22.3 1.0
OD2 A:ASP115 2.5 25.9 1.0
O1A A:UDX801 2.5 42.0 1.0
CG A:ASP115 2.7 24.4 1.0
CG A:ASP112 3.1 26.4 1.0
CE1 A:HIS253 3.2 16.5 1.0
CD2 A:HIS253 3.2 16.5 1.0
PB A:UDX801 3.3 45.6 1.0
CB A:ASP112 3.3 19.3 1.0
PA A:UDX801 3.7 43.2 1.0
O3A A:UDX801 3.8 41.7 1.0
O3D A:UDX801 3.9 35.2 1.0
O2B A:UDX801 4.1 51.8 1.0
C5D A:UDX801 4.1 38.2 1.0
CB A:ASP115 4.2 19.5 1.0
OD1 A:ASP112 4.3 29.2 1.0
ND1 A:HIS253 4.3 15.3 1.0
CG A:HIS253 4.4 14.5 1.0
O5D A:UDX801 4.5 40.1 1.0
O3B A:UDX801 4.5 56.0 1.0
CA A:ASN255 4.7 21.2 1.0
C4D A:UDX801 4.7 36.0 1.0
C3D A:UDX801 4.8 33.1 1.0
O5' A:UDX801 4.8 85.2 1.0
CA A:ASP112 4.9 15.2 1.0
O2A A:UDX801 4.9 47.4 1.0
CB A:ASN255 5.0 24.7 1.0
O A:ASP115 5.0 18.0 1.0
N A:ASP115 5.0 15.5 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: Mon Jul 12 15:18:59 2021

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