Manganese in PDB 4fiy: Crystal Structure of GLFT2 Complexed with Udp

The structure of Crystal Structure of GLFT2 Complexed with Udp, PDB code: 4fiy was solved by R.W.Wheatley, R.B.Zheng, T.L.Lowary, K.K.S.Ng, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 3.10
Space group	P 4 21 2
Cell size a, b, c (Å), α, β, γ (°)	150.398, 150.398, 147.378, 90.00, 90.00, 90.00
R / Rfree (%)	20.7 / 28.7

The binding sites of Manganese atom in the Crystal Structure of GLFT2 Complexed with Udp (pdb code 4fiy). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of GLFT2 Complexed with Udp, PDB code: 4fiy:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of GLFT2 Complexed with Udp


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 GLFT2 Complexed with Udp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn702 b:0.7 occ:1.00 OD2 A:ASP256 1.9 78.4 1.0 NE2 A:HIS396 2.5 76.6 1.0 O1B A:UDP701 2.8 0.5 1.0 OD2 A:ASP258 2.9 90.1 1.0 O1A A:UDP701 2.9 0.8 1.0 OD1 A:ASP258 2.9 84.4 1.0 CE1 A:HIS396 2.9 78.4 1.0 CG A:ASP256 3.0 75.8 1.0 CG A:ASP258 3.3 82.5 1.0 NH2 A:ARG171 3.4 89.4 1.0 O3B A:UDP701 3.5 0.2 1.0 OD1 A:ASP256 3.5 80.1 1.0 PB A:UDP701 3.7 0.1 1.0 CD2 A:HIS396 3.8 75.2 1.0 PA A:UDP701 4.2 0.1 1.0 ND1 A:HIS396 4.2 78.5 1.0 CB A:ASP256 4.3 71.4 1.0 CZ A:ARG171 4.4 92.2 1.0 O3A A:UDP701 4.4 1.0 1.0 CG A:HIS396 4.7 73.7 1.0 C5' A:UDP701 4.7 0.9 1.0 OD1 A:ASP257 4.8 88.4 1.0 NH1 A:ARG171 4.8 92.1 1.0 CB A:ASP258 4.8 76.6 1.0 C3' A:UDP701 4.8 1.0 1.0 O2B A:UDP701 4.9 0.1 1.0 O5' A:UDP701 4.9 0.2 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of GLFT2 Complexed with Udp


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of GLFT2 Complexed with Udp within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn702 b:0.4 occ:1.00 OD1 B:ASP256 2.2 91.3 1.0 NE2 B:HIS396 2.4 88.9 1.0 OD2 B:ASP258 2.7 91.7 1.0 O3B B:UDP701 3.0 0.8 1.0 CG B:ASP256 3.0 91.1 1.0 O1A B:UDP701 3.1 0.3 1.0 CE1 B:HIS396 3.1 89.0 1.0 O5' B:UDP701 3.2 0.9 1.0 OD2 B:ASP256 3.2 96.3 1.0 CG B:ASP258 3.5 91.0 1.0 OD1 B:ASP258 3.5 92.8 1.0 CD2 B:HIS396 3.6 82.4 1.0 NH2 B:ARG171 3.7 0.7 1.0 PA B:UDP701 3.7 0.2 1.0 PB B:UDP701 4.3 0.4 1.0 ND1 B:HIS396 4.3 85.4 1.0 CB B:ASP256 4.4 87.5 1.0 C5' B:UDP701 4.4 0.3 1.0 O3A B:UDP701 4.5 0.8 1.0 C3' B:UDP701 4.6 0.4 1.0 CG B:HIS396 4.6 79.6 1.0 CZ B:ARG171 4.7 0.6 1.0 OD1 B:ASP257 4.7 93.1 1.0 O3' B:UDP701 4.7 0.6 1.0 O2A B:UDP701 5.0 0.4 1.0 CB B:ASP258 5.0 87.8 1.0

R.W.Wheatley, R.B.Zheng, M.R.Richards, T.L.Lowary, K.K.Ng. Tetrameric Structure of the GLFT2 Galactofuranosyltransferase Reveals A Scaffold For the Assembly of Mycobacterial Arabinogalactan. J.Biol.Chem. V. 287 28132 2012.
ISSN: ISSN 0021-9258
PubMed: 22707726
DOI: 10.1074/JBC.M112.347484