Manganese in PDB 5a68: Crystal Structure of the ATTTM3 Product Complex with Two Orthophosphates and Manganese Ions (Form B)

All present enzymatic activity of Crystal Structure of the ATTTM3 Product Complex with Two Orthophosphates and Manganese Ions (Form B):
3.6.1.25; 3.6.1.3;

The structure of Crystal Structure of the ATTTM3 Product Complex with Two Orthophosphates and Manganese Ions (Form B), PDB code: 5a68 was solved by J.Martinez, V.Truffault, M.Hothorn, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.20 / 1.67
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	43.331, 33.811, 71.812, 90.00, 94.40, 90.00
R / Rfree (%)	17.9 / 22.2

The binding sites of Manganese atom in the Crystal Structure of the ATTTM3 Product Complex with Two Orthophosphates and Manganese Ions (Form B) (pdb code 5a68). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 3 binding sites of Manganese where determined in the Crystal Structure of the ATTTM3 Product Complex with Two Orthophosphates and Manganese Ions (Form B), PDB code: 5a68:
Jump to Manganese binding site number: 1; 2; 3;

Manganese binding site 1 out of 3 in the Crystal Structure of the ATTTM3 Product Complex with Two Orthophosphates and Manganese Ions (Form B)


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 the ATTTM3 Product Complex with Two Orthophosphates and Manganese Ions (Form B) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn500 b:19.0 occ:1.00 OE1 A:GLU4 2.0 23.0 1.0 OE2 A:GLU171 2.1 26.9 1.0 O A:HOH2009 2.2 19.6 1.0 O3 A:PO41000 2.3 20.4 1.0 O2 A:PO41000 2.3 20.1 1.0 OE2 A:GLU2 2.4 27.8 1.0 P A:PO41000 2.8 20.7 1.0 CD A:GLU4 3.1 22.9 1.0 CD A:GLU171 3.2 25.9 1.0 CD A:GLU2 3.2 27.9 1.0 MN A:MN502 3.5 23.0 1.0 OE2 A:GLU4 3.5 21.6 1.0 CG A:GLU171 3.6 23.5 1.0 MN A:MN501 3.6 20.9 1.0 OE1 A:GLU169 3.7 24.5 1.0 O A:HOH2005 3.7 22.6 1.0 O1 A:PO41000 3.9 22.7 1.0 OE1 A:GLU2 3.9 30.1 1.0 O4 A:PO41000 3.9 21.9 1.0 CG A:GLU2 3.9 26.5 1.0 O A:HOH2091 4.0 32.6 1.0 OE1 A:GLU171 4.3 27.1 1.0 CG A:GLU4 4.4 21.6 1.0 OE1 A:GLU154 4.5 30.6 1.0 NZ A:LYS76 4.7 21.9 1.0 O A:HOH2046 4.7 46.2 1.0 CB A:GLU4 4.7 20.3 1.0 CD A:GLU169 4.8 25.8 1.0 O A:HOH2049 4.9 41.9 1.0 O A:HOH2093 5.0 31.5 1.0 NH1 A:ARG143 5.0 19.8 1.0

Manganese binding site 2 out of 3 in the Crystal Structure of the ATTTM3 Product Complex with Two Orthophosphates and Manganese Ions (Form B)


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 the ATTTM3 Product Complex with Two Orthophosphates and Manganese Ions (Form B) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn501 b:20.9 occ:1.00 O2 A:PO41001 1.9 33.0 1.0 O3 A:PO41000 2.1 20.4 1.0 OE2 A:GLU4 2.1 21.6 1.0 OE1 A:GLU169 2.2 24.5 1.0 OE2 A:GLU169 2.3 26.1 1.0 O A:HOH2093 2.3 31.5 1.0 CD A:GLU169 2.6 25.8 1.0 O A:HOH2046 2.8 46.2 1.0 CD A:GLU4 3.1 22.9 1.0 P A:PO41001 3.4 36.7 1.0 P A:PO41000 3.4 20.7 1.0 OE1 A:GLU4 3.5 23.0 1.0 MN A:MN500 3.6 19.0 1.0 O A:HOH2009 3.8 19.6 1.0 O4 A:PO41000 3.9 21.9 1.0 O1 A:PO41001 3.9 39.9 1.0 CG A:GLU169 4.0 23.9 1.0 O4 A:PO41001 4.1 33.4 1.0 O A:HOH2045 4.2 27.7 1.0 O1 A:PO41000 4.2 22.7 1.0 NH2 A:ARG143 4.3 20.4 1.0 NZ A:LYS6 4.3 26.5 1.0 O3 A:PO41001 4.4 42.7 1.0 NZ A:LYS200 4.4 25.7 1.0 NZ A:LYS76 4.4 21.9 1.0 O2 A:PO41000 4.4 20.1 1.0 CG A:GLU4 4.5 21.6 1.0 CB A:GLU169 4.7 23.5 1.0 OE1 A:GLU2 4.7 30.1 1.0 OE2 A:GLU2 4.7 27.8 1.0 CD A:LYS6 4.9 24.4 1.0

Manganese binding site 3 out of 3 in the Crystal Structure of the ATTTM3 Product Complex with Two Orthophosphates and Manganese Ions (Form B)


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 the ATTTM3 Product Complex with Two Orthophosphates and Manganese Ions (Form B) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn502 b:23.0 occ:1.00 O A:HOH2005 2.0 22.6 1.0 OE1 A:GLU90 2.1 26.6 1.0 OE2 A:GLU2 2.2 27.8 1.0 O2 A:PO41000 2.2 20.1 1.0 O A:HOH2048 2.2 28.2 1.0 O1 A:PO41000 2.6 22.7 1.0 CD A:GLU90 2.9 23.3 1.0 P A:PO41000 2.9 20.7 1.0 OE2 A:GLU90 3.0 29.4 1.0 CD A:GLU2 3.3 27.9 1.0 MN A:MN500 3.5 19.0 1.0 O3 A:PO41000 3.8 20.4 1.0 NZ A:LYS76 3.8 21.9 1.0 OE2 A:GLU171 3.8 26.9 1.0 CE A:LYS76 3.9 21.6 1.0 O A:HOH2049 3.9 41.9 1.0 OE1 A:GLU2 4.1 30.1 1.0 O4 A:PO41000 4.2 21.9 1.0 CG A:GLU2 4.2 26.5 1.0 NH2 A:ARG52 4.3 25.7 1.0 CG A:GLU90 4.3 20.8 1.0 OE2 A:GLU92 4.4 30.4 1.0 CD A:GLU92 4.6 27.1 1.0 OE1 A:GLU92 4.7 34.0 1.0 O A:HOH2091 4.7 32.6 1.0 CD A:GLU171 4.9 25.9 1.0 CB A:GLU2 4.9 27.6 1.0 CB A:GLU90 4.9 20.2 1.0

J.Martinez, V.Truffault, M.Hothorn. Structural Determinants For Substrate Binding and Catalysis in Triphosphate Tunnel Metalloenzymes. J.Biol.Chem. V. 290 23348 2015.
ISSN: ISSN 0021-9258
PubMed: 26221030
DOI: 10.1074/JBC.M115.674473