Manganese in PDB 1ut5: Divalent Metal Ions (Manganese) Bound to T5 5'-Exonuclease

All present enzymatic activity of Divalent Metal Ions (Manganese) Bound to T5 5'-Exonuclease:
3.1.11.3;

The structure of Divalent Metal Ions (Manganese) Bound to T5 5'-Exonuclease, PDB code: 1ut5 was solved by T.A.Ceska, J.R.Sayers, D.Suck, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25 / 2.75
Space group	P 43
Cell size a, b, c (Å), α, β, γ (°)	77.600, 77.600, 134.610, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Manganese atom in the Divalent Metal Ions (Manganese) Bound to T5 5'-Exonuclease (pdb code 1ut5). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 3 binding sites of Manganese where determined in the Divalent Metal Ions (Manganese) Bound to T5 5'-Exonuclease, PDB code: 1ut5:
Jump to Manganese binding site number: 1; 2; 3;

Manganese binding site 1 out of 3 in the Divalent Metal Ions (Manganese) Bound to T5 5'-Exonuclease


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Divalent Metal Ions (Manganese) Bound to T5 5'-Exonuclease within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1291 b:38.6 occ:1.00 O A:HOH2111 2.4 36.8 1.0 O A:HOH2110 2.4 28.3 1.0 OD2 A:ASP130 3.2 27.1 1.0 O A:HOH2029 3.2 23.5 1.0 OE1 A:GLU128 3.5 24.5 1.0 OD1 A:ASP153 3.9 29.7 1.0 OD2 A:ASP68 3.9 23.2 1.0 O A:HOH2060 3.9 46.5 1.0 CG A:ASP130 4.3 29.0 1.0 OD1 A:ASP68 4.4 26.7 1.0 CG A:ASP68 4.5 24.4 1.0 NE1 A:TRP156 4.6 18.4 1.0 NZ A:LYS83 4.6 28.7 1.0 CD A:GLU128 4.7 22.1 1.0 CB A:ASP130 5.0 25.0 1.0 N A:ASP130 5.0 21.4 1.0 CG A:ASP153 5.0 26.8 1.0

Manganese binding site 2 out of 3 in the Divalent Metal Ions (Manganese) Bound to T5 5'-Exonuclease


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Divalent Metal Ions (Manganese) Bound to T5 5'-Exonuclease within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1292 b:32.9 occ:1.00 OD1 A:ASP155 2.5 23.0 1.0 O A:HOH2084 2.8 23.4 1.0 O A:HOH2085 3.0 9.2 1.0 OD2 A:ASP201 3.0 43.3 1.0 OD2 A:ASP155 3.2 18.1 1.0 OD1 A:ASP201 3.2 41.0 1.0 CG A:ASP155 3.2 18.4 1.0 CG A:ASP201 3.4 40.9 1.0 O A:HOH2059 3.5 71.4 1.0 OD1 A:ASP204 3.8 40.1 1.0 CE A:LYS196 4.2 46.9 1.0 OD2 A:ASP153 4.5 23.3 1.0 CB A:ASP155 4.7 20.2 1.0 CB A:ASP201 4.8 37.9 1.0 CG A:ASP204 4.8 39.1 1.0 O A:HOH2060 4.8 46.5 1.0 NZ A:LYS196 4.8 42.0 1.0

Manganese binding site 3 out of 3 in the Divalent Metal Ions (Manganese) Bound to T5 5'-Exonuclease


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Divalent Metal Ions (Manganese) Bound to T5 5'-Exonuclease within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn1292 b:32.2 occ:1.00 O B:HOH2062 2.6 71.0 1.0 OD1 B:ASP130 3.2 26.6 1.0 OD2 B:ASP130 3.4 26.6 1.0 CG B:ASP130 3.6 24.8 1.0 OD2 B:ASP68 3.7 23.0 1.0 OD1 B:ASP68 4.1 15.6 1.0 CG B:ASP68 4.2 22.8 1.0 OD1 B:ASP153 4.4 32.2 1.0 OE2 B:GLU128 4.5 26.9 1.0 NE1 B:TRP156 4.6 27.1 1.0 OD2 B:ASP26 4.6 19.6 1.0 CB B:ALA129 4.6 20.7 1.0 N B:ALA129 4.7 23.4 1.0 N B:ASP130 4.8 23.2 1.0 NZ B:LYS83 4.8 13.0 1.0

M.Feng, D.Patel, J.Dervan, T.A.Ceska, D.Suck, I.Haq, J.R.Sayers. Roles of Divalent Metal Ions in Flap Endonuclease-Substrate Interactions Nat.Struct.Mol.Biol. V. 11 450 2004.
ISSN: ISSN 1545-9993
PubMed: 15077103
DOI: 10.1038/NSMB754