Manganese in PDB 4uc5: Neisseria Meningitidis DAH7PS-Phenylalanine Regulated

All present enzymatic activity of Neisseria Meningitidis DAH7PS-Phenylalanine Regulated:
2.5.1.54;

The structure of Neisseria Meningitidis DAH7PS-Phenylalanine Regulated, PDB code: 4uc5 was solved by L.C.Heyes, E.J.M.Lang, E.J.Parker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	74.74 / 2.19
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	73.607, 143.460, 75.179, 90.00, 96.18, 90.00
R / Rfree (%)	18.904 / 23.57

The binding sites of Manganese atom in the Neisseria Meningitidis DAH7PS-Phenylalanine Regulated (pdb code 4uc5). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Neisseria Meningitidis DAH7PS-Phenylalanine Regulated, PDB code: 4uc5:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in the Neisseria Meningitidis DAH7PS-Phenylalanine Regulated


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Neisseria Meningitidis DAH7PS-Phenylalanine Regulated within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1350 b:43.6 occ:1.00 O A:HOH2028 2.0 52.0 1.0 OD2 A:ASP324 2.0 35.1 1.0 OE2 A:GLU304 2.2 41.0 1.0 NE2 A:HIS270 2.3 41.5 1.0 SG A:CYS63 2.5 44.0 1.0 CD A:GLU304 2.9 40.3 1.0 OE1 A:GLU304 3.0 40.8 1.0 CG A:ASP324 3.1 36.4 1.0 CE1 A:HIS270 3.3 41.1 1.0 CD2 A:HIS270 3.3 40.2 1.0 CB A:CYS63 3.5 43.2 1.0 CB A:ASP324 3.5 37.6 1.0 NH2 A:ARG94 3.9 40.3 1.0 NZ A:LYS99 4.1 59.2 1.0 OD1 A:ASP324 4.1 38.0 1.0 O A:HOH2106 4.2 44.7 1.0 CA A:CYS63 4.2 43.1 1.0 CG A:GLU304 4.4 41.2 1.0 ND1 A:HIS270 4.4 38.6 1.0 O A:HOH2027 4.4 40.1 1.0 CG A:HIS270 4.4 39.6 1.0 O A:HOH2038 4.5 38.4 1.0 CZ A:ARG94 4.7 41.3 1.0 CG A:LYS99 4.7 59.3 1.0 O A:CYS63 4.8 37.9 1.0 CA A:ASP324 4.8 37.5 1.0 C A:CYS63 4.9 41.6 1.0 CD A:LYS99 4.9 62.6 1.0 N A:ASP324 4.9 36.1 1.0

Manganese binding site 2 out of 4 in the Neisseria Meningitidis DAH7PS-Phenylalanine Regulated


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Neisseria Meningitidis DAH7PS-Phenylalanine Regulated within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn1350 b:60.5 occ:1.00 OD2 B:ASP324 2.0 53.8 1.0 OE2 B:GLU304 2.1 51.1 1.0 NE2 B:HIS270 2.5 55.5 1.0 SG B:CYS63 2.6 56.2 1.0 CG B:ASP324 2.9 57.9 1.0 CD B:GLU304 2.9 51.3 1.0 OE1 B:GLU304 3.2 53.2 1.0 CB B:ASP324 3.3 56.9 1.0 CD2 B:HIS270 3.4 57.0 1.0 CE1 B:HIS270 3.5 55.8 1.0 CB B:CYS63 3.5 57.5 1.0 NH2 B:ARG94 3.9 52.9 1.0 OD1 B:ASP324 4.0 57.3 1.0 CA B:CYS63 4.1 53.4 1.0 O B:HOH2014 4.1 45.9 1.0 CG B:GLU304 4.4 49.3 1.0 NZ B:LYS99 4.5 70.6 1.0 O B:CYS63 4.6 47.0 1.0 O B:HOH2023 4.6 41.0 1.0 ND1 B:HIS270 4.6 57.1 1.0 CG B:HIS270 4.6 58.1 1.0 CA B:ASP324 4.6 59.8 1.0 CZ B:ARG94 4.6 49.7 1.0 C B:CYS63 4.7 50.5 1.0 N B:ASP324 4.7 58.0 1.0 NH1 B:ARG94 4.8 51.3 1.0 CG B:LYS99 4.8 64.7 1.0 CD B:LYS99 5.0 69.5 1.0 O1 B:SO41351 5.0 90.0 1.0

Manganese binding site 3 out of 4 in the Neisseria Meningitidis DAH7PS-Phenylalanine Regulated


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Neisseria Meningitidis DAH7PS-Phenylalanine Regulated within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn1350 b:50.9 occ:1.00 OE2 C:GLU304 1.9 42.6 1.0 OD2 C:ASP324 2.1 51.3 1.0 NE2 C:HIS270 2.4 58.1 1.0 SG C:CYS63 2.7 47.5 1.0 CD C:GLU304 3.0 44.3 1.0 CG C:ASP324 3.1 56.7 1.0 CE1 C:HIS270 3.3 57.4 1.0 OE1 C:GLU304 3.3 46.3 1.0 CD2 C:HIS270 3.3 58.8 1.0 CB C:ASP324 3.5 57.9 1.0 CB C:CYS63 3.5 45.5 1.0 NH2 C:ARG94 4.0 51.8 1.0 O C:HOH2087 4.0 46.7 1.0 CA C:CYS63 4.1 46.1 1.0 NZ C:LYS99 4.2 65.2 1.0 OD1 C:ASP324 4.2 58.9 1.0 CG C:GLU304 4.3 42.2 1.0 ND1 C:HIS270 4.4 58.5 1.0 CG C:HIS270 4.4 58.6 1.0 CG C:LYS99 4.6 60.8 1.0 O C:CYS63 4.6 47.1 1.0 CD C:LYS99 4.6 66.0 1.0 C C:CYS63 4.7 48.0 1.0 CA C:ASP324 4.7 60.1 1.0 N C:ASP324 4.8 58.1 1.0 CZ C:ARG94 5.0 51.6 1.0 CE C:LYS99 5.0 66.4 1.0

Manganese binding site 4 out of 4 in the Neisseria Meningitidis DAH7PS-Phenylalanine Regulated


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Neisseria Meningitidis DAH7PS-Phenylalanine Regulated within 5.0Å range: probe atom residue distance (Å) B Occ D:Mn1350 b:56.5 occ:1.00 OE2 D:GLU304 1.8 53.1 1.0 OD2 D:ASP324 2.1 45.7 1.0 NE2 D:HIS270 2.4 58.3 1.0 SG D:CYS63 2.6 51.6 1.0 CD D:GLU304 2.9 52.6 1.0 CG D:ASP324 3.2 48.6 1.0 OE1 D:GLU304 3.3 57.8 1.0 CE1 D:HIS270 3.4 60.6 1.0 CD2 D:HIS270 3.4 58.5 1.0 CB D:CYS63 3.6 50.8 1.0 CB D:ASP324 3.8 48.5 1.0 NH1 D:ARG94 4.2 56.7 1.0 NZ D:LYS99 4.2 65.8 1.0 CA D:CYS63 4.2 50.0 1.0 CG D:GLU304 4.2 50.2 1.0 OD1 D:ASP324 4.2 45.3 1.0 ND1 D:HIS270 4.5 60.1 1.0 CG D:HIS270 4.5 60.3 1.0 CG D:LYS99 4.5 64.6 1.0 O D:CYS63 4.6 50.7 1.0 CD D:LYS99 4.7 71.1 1.0 C D:CYS63 4.7 49.6 1.0 CZ D:ARG94 4.8 58.0 1.0 O4 D:SO41351 4.9 88.8 1.0 NH2 D:ARG94 4.9 63.6 1.0 N D:ASP324 5.0 47.9 1.0

E.J.Lang, L.C.Heyes, G.B.Jameson, E.J.Parker. Calculated Pka Variations Expose Dynamic Allosteric Communication Networks. J.Am.Chem.Soc. V. 138 2036 2016.
ISSN: ISSN 0002-7863
PubMed: 26794122
DOI: 10.1021/JACS.5B13134