Manganese in PDB 9g1a: Fragment Screening of Fosakp, Room-Temperature Structure, Ground State

The structure of Fragment Screening of Fosakp, Room-Temperature Structure, Ground State, PDB code: 9g1a was solved by S.Guenther, M.Galchenkova, P.Fischer, P.Y.A.Reinke, S.Falke, S.Thekkuveedu, A.C.Rodrigues, J.Senst, A.Meents, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.85 / 1.30
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	71.62, 91.69, 45.3, 90, 90, 90
R / Rfree (%)	13.8 / 15.7

The binding sites of Manganese atom in the Fragment Screening of Fosakp, Room-Temperature Structure, Ground State (pdb code 9g1a). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Fragment Screening of Fosakp, Room-Temperature Structure, Ground State, PDB code: 9g1a:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Fragment Screening of Fosakp, Room-Temperature Structure, Ground State


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Fragment Screening of Fosakp, Room-Temperature Structure, Ground State within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn201 b:13.3 occ:1.00 OE1 A:GLU113 2.0 15.7 1.0 OE2 A:GLU98 2.1 19.1 1.0 NE2 A:HIS67 2.1 13.0 1.0 NE2 B:HIS7 2.1 14.5 1.0 CD A:GLU98 2.8 22.7 1.0 OE1 A:GLU98 2.9 30.1 1.0 O A:HOH303 2.9 20.5 1.0 CD A:GLU113 2.9 14.1 1.0 CE1 B:HIS7 3.0 13.5 1.0 CD2 A:HIS67 3.1 12.5 1.0 HE1 B:HIS7 3.1 16.2 1.0 CE1 A:HIS67 3.1 12.5 1.0 OE2 A:GLU113 3.2 15.6 1.0 CD2 B:HIS7 3.2 13.2 1.0 HD2 A:HIS67 3.2 14.9 1.0 HE1 A:HIS67 3.3 15.0 1.0 HD2 B:HIS7 3.4 15.8 1.0 HE1 A:TYR103 3.5 20.8 1.0 HB2 A:ALA69 3.6 17.9 1.0 HD22 A:LEU94 3.9 41.3 1.0 OG1 B:THR9 4.1 15.0 1.0 ND1 B:HIS7 4.2 12.9 1.0 HG1 B:THR9 4.2 18.0 1.0 CG A:GLU98 4.2 22.9 1.0 ND1 A:HIS67 4.2 12.9 1.0 CG A:HIS67 4.2 11.6 1.0 CG B:HIS7 4.3 13.3 1.0 CG A:GLU113 4.3 14.8 1.0 CE1 A:TYR103 4.3 17.4 1.0 HG3 A:GLU98 4.4 27.5 1.0 OH A:TYR103 4.4 21.9 1.0 HB3 A:GLU113 4.4 15.3 1.0 CB A:ALA69 4.5 14.9 1.0 HB2 A:GLU113 4.5 15.3 1.0 HD21 A:LEU94 4.5 41.3 1.0 HG2 A:GLU98 4.6 27.5 1.0 CD2 A:LEU94 4.6 34.4 1.0 HG A:SER101 4.6 24.9 1.0 HB3 A:ALA69 4.7 17.9 1.0 CB A:GLU113 4.7 12.8 1.0 HD23 A:LEU94 4.7 41.3 1.0 HB1 A:ALA69 4.8 17.9 1.0 HG B:CYS48 4.8 17.3 0.3 HB B:THR9 4.8 15.8 1.0 HG3 A:GLU113 4.8 17.7 1.0 HG2 A:GLU113 4.9 17.7 1.0 CZ A:TYR103 4.9 19.4 1.0 HD1 B:HIS7 4.9 15.4 1.0 HH A:TYR103 4.9 26.3 1.0

Manganese binding site 2 out of 2 in the Fragment Screening of Fosakp, Room-Temperature Structure, Ground State


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Fragment Screening of Fosakp, Room-Temperature Structure, Ground State within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn201 b:13.7 occ:1.00 O B:HOH386 2.0 27.8 1.0 OE1 B:GLU113 2.1 14.0 1.0 NE2 B:HIS67 2.1 13.5 1.0 NE2 A:HIS7 2.2 13.0 1.0 O B:HOH307 2.3 26.0 1.0 O A:HOH376 2.6 17.9 1.0 CE1 A:HIS7 3.0 13.2 1.0 CD B:GLU113 3.1 13.5 1.0 CE1 B:HIS67 3.1 12.3 1.0 HE1 A:HIS7 3.1 15.8 1.0 CD2 B:HIS67 3.1 13.0 1.0 CD2 A:HIS7 3.3 12.4 1.0 HE1 B:HIS67 3.3 14.7 1.0 HD2 B:HIS67 3.3 15.6 1.0 OE2 B:GLU113 3.4 15.9 1.0 HE1 B:TYR103 3.5 20.1 1.0 HD2 A:HIS7 3.5 14.8 1.0 HG1 A:THR9 3.6 16.7 1.0 HB2 B:ALA69 3.7 15.7 1.0 OG1 A:THR9 4.0 13.9 1.0 ND1 A:HIS7 4.2 12.5 1.0 ND1 B:HIS67 4.2 12.5 1.0 CG B:HIS67 4.3 11.0 1.0 CE1 B:TYR103 4.3 16.8 1.0 CG A:HIS7 4.3 11.8 1.0 OH B:TYR103 4.4 21.9 1.0 CG B:GLU113 4.4 13.8 1.0 HB3 B:GLU113 4.4 15.4 1.0 HB2 B:GLU113 4.5 15.4 1.0 CB B:ALA69 4.6 13.1 1.0 HH B:TYR65 4.6 29.2 1.0 HB A:THR9 4.7 13.8 1.0 CB B:GLU113 4.7 12.8 1.0 HB3 B:ALA69 4.8 15.7 1.0 HB1 B:ALA69 4.8 15.7 1.0 HG3 B:GLU113 4.9 16.6 1.0 CZ B:TYR103 4.9 17.5 1.0 CB A:THR9 4.9 11.6 1.0 HD1 A:HIS7 5.0 15.0 1.0 OH B:TYR65 5.0 24.3 1.0 HG2 B:GLU113 5.0 16.6 1.0 HH B:TYR103 5.0 26.3 1.0

S.Guenther, A.Meents. Room Temperature X-Ray Fragment Screening with Serial Crystallography To Be Published.