Manganese in PDB 3tux: Crystal Structure of Rtca.Atp.Mn Ternary Complex

All present enzymatic activity of Crystal Structure of Rtca.Atp.Mn Ternary Complex:
6.5.1.4;

The structure of Crystal Structure of Rtca.Atp.Mn Ternary Complex, PDB code: 3tux was solved by A.K.Chakravarty, P.Smith, S.Shuman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	26.66 / 1.85
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	69.530, 83.060, 52.080, 90.00, 90.00, 90.00
R / Rfree (%)	18.5 / 25.2

The binding sites of Manganese atom in the Crystal Structure of Rtca.Atp.Mn Ternary Complex (pdb code 3tux). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Crystal Structure of Rtca.Atp.Mn Ternary Complex, PDB code: 3tux:

Manganese binding site 1 out of 1 in the Crystal Structure of Rtca.Atp.Mn Ternary Complex


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 Rtca.Atp.Mn Ternary Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn601 b:34.7 occ:1.00 O1B A:ATP501 2.3 37.9 1.0 OE2 A:GLU14 2.3 30.6 1.0 O1G A:ATP501 2.3 33.3 1.0 O2A A:ATP501 2.4 32.8 1.0 O A:HOH392 2.4 26.4 1.0 O A:HOH418 2.6 34.6 1.0 PA A:ATP501 3.1 28.8 1.0 PB A:ATP501 3.2 43.0 1.0 CD A:GLU14 3.4 32.5 1.0 O3A A:ATP501 3.4 38.5 1.0 PG A:ATP501 3.6 38.0 1.0 O1A A:ATP501 3.6 32.1 1.0 O3B A:ATP501 3.7 42.9 1.0 OE1 A:GLU14 3.7 27.9 1.0 NH2 A:ARG43 3.9 34.2 1.0 O A:HOH595 4.2 38.8 1.0 O A:HOH386 4.4 23.0 1.0 O3G A:ATP501 4.5 39.5 1.0 ND2 A:ASN309 4.5 21.0 1.0 OG A:SER129 4.5 43.5 1.0 O A:HOH549 4.6 39.2 1.0 O5' A:ATP501 4.6 31.5 1.0 O2B A:ATP501 4.6 39.7 1.0 O2G A:ATP501 4.6 26.7 1.0 CG A:GLU14 4.7 31.4 1.0 O A:HOH470 4.8 27.1 1.0 C5' A:ATP501 4.9 17.7 1.0 CZ A:ARG43 5.0 35.2 1.0

A.K.Chakravarty, P.Smith, S.Shuman. Structures of Rna 3'-Phosphate Cyclase Bound to Atp Reveal the Mechanism of Nucleotidyl Transfer and Metal-Assisted Catalysis. Proc.Natl.Acad.Sci.Usa V. 108 21034 2011.
ISSN: ISSN 0027-8424
PubMed: 22167800
DOI: 10.1073/PNAS.1115560108