Manganese in PDB 6sna: Crystal Structure of Antirestriction Ardc Protein From R388 Plasmid. Mn(II)-Bound Structure.

The structure of Crystal Structure of Antirestriction Ardc Protein From R388 Plasmid. Mn(II)-Bound Structure., PDB code: 6sna was solved by L.Gonzalez-Montes, G.Moncalian, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	54.82 / 2.70
Space group	P 32
Cell size a, b, c (Å), α, β, γ (°)	116.499, 116.499, 162.123, 90.00, 90.00, 120.00
R / Rfree (%)	22.2 / 29.4

The binding sites of Manganese atom in the Crystal Structure of Antirestriction Ardc Protein From R388 Plasmid. Mn(II)-Bound Structure. (pdb code 6sna). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 8 binding sites of Manganese where determined in the Crystal Structure of Antirestriction Ardc Protein From R388 Plasmid. Mn(II)-Bound Structure., PDB code: 6sna:
Jump to Manganese binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Manganese binding site 1 out of 8 in the Crystal Structure of Antirestriction Ardc Protein From R388 Plasmid. Mn(II)-Bound Structure.


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 Antirestriction Ardc Protein From R388 Plasmid. Mn(II)-Bound Structure. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn401 b:40.4 occ:1.00 NE2 A:HIS205 1.8 22.2 1.0 OE2 A:GLU229 1.9 22.4 1.0 NE2 A:HIS201 2.2 23.8 1.0 CD A:GLU229 2.4 25.7 1.0 CD2 A:HIS205 2.4 21.4 1.0 OE1 A:GLU229 2.4 24.7 1.0 CD2 A:HIS201 2.9 22.4 1.0 CE1 A:HIS205 3.1 26.4 1.0 CE1 A:HIS201 3.2 25.3 1.0 CG A:HIS205 3.6 18.5 1.0 CG A:GLU229 3.8 26.8 1.0 ND1 A:HIS205 3.9 22.3 1.0 CG A:HIS201 4.1 24.7 1.0 ND1 A:HIS201 4.2 25.1 1.0 OE2 A:GLU202 4.3 31.3 1.0 OE1 A:GLU202 4.4 26.5 1.0 CB A:ALA232 4.7 21.5 1.0 CD A:GLU202 4.7 26.5 1.0 O A:HOH540 4.8 43.7 1.0 CB A:GLU229 4.8 26.2 1.0 CB A:HIS205 4.9 16.4 1.0 O A:HIS201 5.0 24.6 1.0

Manganese binding site 2 out of 8 in the Crystal Structure of Antirestriction Ardc Protein From R388 Plasmid. Mn(II)-Bound Structure.


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 Antirestriction Ardc Protein From R388 Plasmid. Mn(II)-Bound Structure. within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn401 b:32.2 occ:1.00 OE1 B:GLU229 2.0 31.0 1.0 NE2 B:HIS201 2.2 27.4 1.0 NE2 B:HIS205 2.4 23.3 1.0 O B:HOH529 2.5 29.1 1.0 CD B:GLU229 2.6 45.4 1.0 OE2 B:GLU229 2.8 58.8 1.0 CD2 B:HIS201 3.0 26.6 1.0 CD2 B:HIS205 3.1 22.4 1.0 CE1 B:HIS201 3.3 26.7 1.0 CE1 B:HIS205 3.5 28.8 1.0 CG B:GLU229 4.0 42.1 1.0 CG B:HIS201 4.2 27.4 1.0 CG B:HIS205 4.3 24.8 1.0 ND1 B:HIS201 4.4 28.4 1.0 OE2 B:GLU202 4.4 35.9 1.0 ND1 B:HIS205 4.5 24.5 1.0 CB B:GLU229 4.7 35.3 1.0 OE1 B:GLU202 4.9 32.9 1.0

Manganese binding site 3 out of 8 in the Crystal Structure of Antirestriction Ardc Protein From R388 Plasmid. Mn(II)-Bound Structure.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of Antirestriction Ardc Protein From R388 Plasmid. Mn(II)-Bound Structure. within 5.0Å range: probe atom residue distance (Å) B Occ F:Mn401 b:73.7 occ:1.00 NE2 F:HIS201 1.8 61.1 1.0 NE2 F:HIS205 1.9 63.4 1.0 OE2 F:GLU229 2.0 62.6 1.0 CD2 F:HIS205 2.3 63.9 1.0 OE1 F:GLU229 2.4 50.4 1.0 CD F:GLU229 2.5 58.2 1.0 CD2 F:HIS201 2.6 52.3 1.0 CE1 F:HIS201 2.9 56.9 1.0 CE1 F:HIS205 3.2 62.7 1.0 CG F:HIS205 3.6 62.0 1.0 CG F:HIS201 3.8 52.3 1.0 CG F:GLU229 3.9 61.9 1.0 ND1 F:HIS201 3.9 52.7 1.0 ND1 F:HIS205 4.0 60.9 1.0 OE2 F:GLU202 4.2 53.2 1.0 OE1 F:GLU202 4.3 53.5 1.0 CB F:ALA232 4.4 52.3 1.0 CD F:GLU202 4.6 53.3 1.0 CB F:GLU229 4.8 57.0 1.0 CB F:HIS205 4.9 61.5 1.0

Manganese binding site 4 out of 8 in the Crystal Structure of Antirestriction Ardc Protein From R388 Plasmid. Mn(II)-Bound Structure.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystal Structure of Antirestriction Ardc Protein From R388 Plasmid. Mn(II)-Bound Structure. within 5.0Å range: probe atom residue distance (Å) B Occ G:Mn401 b:46.1 occ:1.00 NE2 G:HIS201 1.9 40.0 1.0 OE2 G:GLU229 1.9 29.2 1.0 NE2 G:HIS205 1.9 29.9 1.0 O G:HOH505 2.0 45.2 1.0 CD G:GLU229 2.5 36.9 1.0 CD2 G:HIS205 2.6 20.6 1.0 OE1 G:GLU229 2.7 40.0 1.0 CD2 G:HIS201 2.8 29.0 1.0 CE1 G:HIS201 2.8 28.4 1.0 CE1 G:HIS205 3.1 31.1 1.0 CG G:HIS205 3.8 20.6 1.0 ND1 G:HIS201 3.9 28.5 1.0 CG G:HIS201 3.9 27.4 1.0 CG G:GLU229 3.9 31.6 1.0 ND1 G:HIS205 4.1 26.4 1.0 OE2 G:GLU202 4.2 35.6 1.0 CB G:ALA232 4.6 22.6 1.0 OE1 G:GLU202 4.8 33.0 1.0 CD G:GLU202 4.9 27.6 1.0 CB G:GLU229 4.9 29.6 1.0

Manganese binding site 5 out of 8 in the Crystal Structure of Antirestriction Ardc Protein From R388 Plasmid. Mn(II)-Bound Structure.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 5 of Crystal Structure of Antirestriction Ardc Protein From R388 Plasmid. Mn(II)-Bound Structure. within 5.0Å range: probe atom residue distance (Å) B Occ J:Mn401 b:52.9 occ:1.00 NE2 J:HIS205 1.8 58.3 1.0 OE2 J:GLU229 1.8 57.5 1.0 NE2 J:HIS201 2.0 54.4 1.0 O J:HOH502 2.0 49.4 1.0 CD J:GLU229 2.1 60.0 1.0 OE1 J:GLU229 2.3 57.4 1.0 CD2 J:HIS205 2.4 57.6 1.0 CD2 J:HIS201 2.8 52.1 1.0 CE1 J:HIS205 3.0 56.2 1.0 CE1 J:HIS201 3.0 53.5 1.0 CG J:GLU229 3.3 53.4 1.0 CG J:HIS205 3.7 57.5 1.0 ND1 J:HIS205 3.9 48.4 1.0 CG J:HIS201 4.0 50.5 1.0 ND1 J:HIS201 4.0 52.8 1.0 OE2 J:GLU202 4.1 56.4 1.0 CB J:GLU229 4.3 53.7 1.0 CB J:ALA232 4.6 49.0 1.0 OE1 J:GLU202 4.7 50.9 1.0 CD J:GLU202 4.8 54.8 1.0 CA J:GLU229 4.9 58.6 1.0

Manganese binding site 6 out of 8 in the Crystal Structure of Antirestriction Ardc Protein From R388 Plasmid. Mn(II)-Bound Structure.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 6 of Crystal Structure of Antirestriction Ardc Protein From R388 Plasmid. Mn(II)-Bound Structure. within 5.0Å range: probe atom residue distance (Å) B Occ K:Mn401 b:45.1 occ:1.00 OE2 K:GLU229 1.9 40.9 1.0 NE2 K:HIS201 2.2 33.9 1.0 NE2 K:HIS205 2.4 27.7 1.0 OE1 K:GLU229 2.4 53.3 1.0 CD K:GLU229 2.5 42.7 1.0 CD2 K:HIS205 2.9 24.2 1.0 CD2 K:HIS201 3.1 32.4 1.0 CE1 K:HIS201 3.3 32.2 1.0 CE1 K:HIS205 3.6 30.1 1.0 CG K:GLU229 3.9 35.9 1.0 CG K:HIS205 4.2 24.6 1.0 CG K:HIS201 4.3 26.1 1.0 ND1 K:HIS201 4.3 28.9 1.0 OE2 K:GLU202 4.4 31.1 1.0 ND1 K:HIS205 4.5 30.1 1.0 OE1 K:GLU202 4.6 30.7 1.0 CD K:GLU202 4.9 27.3 1.0 CB K:GLU229 5.0 30.0 1.0

Manganese binding site 7 out of 8 in the Crystal Structure of Antirestriction Ardc Protein From R388 Plasmid. Mn(II)-Bound Structure.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 7 of Crystal Structure of Antirestriction Ardc Protein From R388 Plasmid. Mn(II)-Bound Structure. within 5.0Å range: probe atom residue distance (Å) B Occ N:Mn401 b:60.8 occ:1.00 OE2 N:GLU229 1.7 44.9 1.0 CE1 N:HIS205 1.8 64.5 1.0 CD N:GLU229 2.2 50.4 1.0 OE1 N:GLU229 2.2 56.9 1.0 NE2 N:HIS205 2.3 58.8 1.0 NE2 N:HIS201 2.5 55.8 1.0 ND1 N:HIS205 3.0 59.3 1.0 CE1 N:HIS201 3.3 51.1 1.0 CD2 N:HIS201 3.4 50.3 1.0 CD2 N:HIS205 3.6 58.3 1.0 CG N:GLU229 3.7 48.8 1.0 CG N:HIS205 3.9 56.7 1.0 OE2 N:GLU202 4.4 57.6 1.0 ND1 N:HIS201 4.4 51.8 1.0 CG N:HIS201 4.5 51.1 1.0 OE1 N:GLU202 4.6 58.1 1.0 CB N:GLU229 4.7 51.0 1.0 CB N:ALA232 4.8 42.5 1.0 CD N:GLU202 4.9 57.8 1.0

Manganese binding site 8 out of 8 in the Crystal Structure of Antirestriction Ardc Protein From R388 Plasmid. Mn(II)-Bound Structure.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 8 of Crystal Structure of Antirestriction Ardc Protein From R388 Plasmid. Mn(II)-Bound Structure. within 5.0Å range: probe atom residue distance (Å) B Occ X:Mn401 b:49.6 occ:1.00 NE2 X:HIS205 1.9 51.0 1.0 OE2 X:GLU229 1.9 49.3 1.0 NE2 X:HIS201 2.0 43.9 1.0 O X:HOH515 2.3 46.8 1.0 CD X:GLU229 2.3 54.2 1.0 OE1 X:GLU229 2.3 61.0 1.0 CD2 X:HIS205 2.5 47.0 1.0 CD2 X:HIS201 2.6 46.5 1.0 CE1 X:HIS205 3.0 50.2 1.0 CE1 X:HIS201 3.1 46.4 1.0 CG X:HIS201 3.7 41.2 1.0 CG X:GLU229 3.8 52.1 1.0 CG X:HIS205 3.8 47.4 1.0 ND1 X:HIS201 3.9 45.0 1.0 ND1 X:HIS205 4.0 49.0 1.0 O X:HOH527 4.2 45.6 1.0 OE2 X:GLU202 4.4 47.6 1.0 OE1 X:GLU202 4.5 49.5 1.0 CB X:ALA232 4.5 42.6 1.0 CB X:GLU229 4.7 52.8 1.0 CD X:GLU202 4.9 48.4 1.0

L.Gonzalez-Montes, G.Moncalian. Crystal Structure of Antirestriction Ardc Protein From R388 Plasmid. To Be Published.