Manganese in PDB 5xhp: Transferase with Ligands

The structure of Transferase with Ligands, PDB code: 5xhp was solved by J.Park, Y.Yoo, Y.H.Kim, H.S.Cho, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.40 / 2.80
Space group	P 32
Cell size a, b, c (Å), α, β, γ (°)	50.116, 50.116, 201.704, 90.00, 90.00, 120.00
R / Rfree (%)	28.8 / 31.9

The binding sites of Manganese atom in the Transferase with Ligands (pdb code 5xhp). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Transferase with Ligands, PDB code: 5xhp:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Transferase with Ligands


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Transferase with Ligands within 5.0Å range: probe atom residue distance (Å) B Occ F:Mn402 b:60.0 occ:1.00 OG F:SER340 1.7 61.0 1.0 O1B F:UDP403 2.2 51.7 1.0 OD1 F:ASN338 2.2 71.9 1.0 O1A F:UDP403 2.2 65.2 1.0 OD2 F:ASP241 2.5 69.0 1.0 CB F:SER340 3.1 67.4 1.0 CG F:ASP241 3.3 68.4 1.0 OD1 F:ASP241 3.4 70.2 1.0 CG F:ASN338 3.4 72.0 1.0 PA F:UDP403 3.6 66.6 1.0 PB F:UDP403 3.6 58.4 1.0 CD F:ARG401 3.9 76.4 1.0 O3A F:UDP403 4.0 57.9 1.0 N F:ARG401 4.0 78.1 1.0 N F:SER340 4.1 74.0 1.0 CA F:SER340 4.1 66.8 1.0 NH1 F:ARG401 4.2 73.5 1.0 CB F:ASN338 4.3 71.5 1.0 CA F:ASN338 4.3 69.8 1.0 ND2 F:ASN338 4.4 66.2 1.0 NE F:ARG401 4.4 75.3 1.0 OD2 F:ASP239 4.4 64.7 1.0 O3B F:UDP403 4.4 56.6 1.0 C5' F:UDP403 4.4 67.8 1.0 O5' F:UDP403 4.5 67.8 1.0 CZ F:ARG401 4.5 71.7 1.0 C F:ASN338 4.5 68.5 1.0 O2B F:UDP403 4.6 57.2 1.0 CB F:ASP241 4.7 65.9 1.0 O2A F:UDP403 4.7 67.6 1.0 C F:SER340 4.7 64.0 1.0 OH F:TYR88 4.7 87.1 1.0 N F:SER341 4.7 67.8 1.0 O F:ASN338 4.8 77.6 1.0 N F:THR339 5.0 66.9 1.0

Manganese binding site 2 out of 2 in the Transferase with Ligands


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Transferase with Ligands within 5.0Å range: probe atom residue distance (Å) B Occ E:Mn402 b:67.8 occ:1.00 OG E:SER340 1.7 57.3 1.0 OD1 E:ASN338 2.1 62.2 1.0 O2B E:UDP403 2.2 52.6 1.0 O2A E:UDP403 2.2 60.5 1.0 OD2 E:ASP241 2.5 69.8 1.0 CB E:SER340 3.1 63.3 1.0 CG E:ASP241 3.3 69.2 1.0 CG E:ASN338 3.4 66.3 1.0 OD1 E:ASP241 3.5 74.2 1.0 PA E:UDP403 3.6 63.5 1.0 PB E:UDP403 3.6 54.4 1.0 OD2 E:ASP239 3.7 63.5 1.0 N E:ARG401 3.9 76.4 1.0 CD E:ARG401 3.9 72.4 1.0 O3A E:UDP403 3.9 51.9 1.0 N E:SER340 4.0 70.4 1.0 CA E:SER340 4.1 61.1 1.0 CB E:ASN338 4.2 68.1 1.0 NH2 E:ARG401 4.3 65.8 1.0 CA E:ASN338 4.3 68.0 1.0 ND2 E:ASN338 4.3 64.3 1.0 C E:ASN338 4.5 64.3 1.0 O1B E:UDP403 4.5 50.8 1.0 O3B E:UDP403 4.5 60.3 1.0 NE E:ARG401 4.5 72.2 1.0 C5' E:UDP403 4.5 61.6 1.0 O5' E:UDP403 4.6 63.2 1.0 O1A E:UDP403 4.6 65.4 1.0 C E:SER340 4.6 56.5 1.0 N E:SER341 4.6 56.5 1.0 CZ E:ARG401 4.7 66.0 1.0 OH E:TYR88 4.7 79.3 1.0 CB E:ASP241 4.7 67.1 1.0 O E:ASN338 4.8 67.9 1.0 CG E:ASP239 4.8 64.6 1.0 CB E:ARG401 4.9 77.9 1.0 N E:THR339 5.0 60.5 1.0 CG E:ARG401 5.0 74.5 1.0

J.Park, Y.Yoo, H.S.Cho. Crystal Structure of L-Arginine and Udp Bounded Glycosyltransfease To Be Published.