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Manganese in PDB 3x0n: Adp Ribose Pyrophosphatase From Thermus Thermophilus HB8 in Esm-State at Reaction Time of 6 Min

Enzymatic activity of Adp Ribose Pyrophosphatase From Thermus Thermophilus HB8 in Esm-State at Reaction Time of 6 Min

All present enzymatic activity of Adp Ribose Pyrophosphatase From Thermus Thermophilus HB8 in Esm-State at Reaction Time of 6 Min:
3.6.1.13;

Protein crystallography data

The structure of Adp Ribose Pyrophosphatase From Thermus Thermophilus HB8 in Esm-State at Reaction Time of 6 Min, PDB code: 3x0n was solved by Y.Furuike, Y.Akita, I.Miyahara, N.Kamiya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.12
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 49.687, 49.687, 118.974, 90.00, 90.00, 120.00
R / Rfree (%) 15.2 / n/a

Manganese Binding Sites:

The binding sites of Manganese atom in the Adp Ribose Pyrophosphatase From Thermus Thermophilus HB8 in Esm-State at Reaction Time of 6 Min (pdb code 3x0n). 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 Adp Ribose Pyrophosphatase From Thermus Thermophilus HB8 in Esm-State at Reaction Time of 6 Min, PDB code: 3x0n:

Manganese binding site 1 out of 1 in 3x0n

Go back to Manganese Binding Sites List in 3x0n
Manganese binding site 1 out of 1 in the Adp Ribose Pyrophosphatase From Thermus Thermophilus HB8 in Esm-State at Reaction Time of 6 Min


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Adp Ribose Pyrophosphatase From Thermus Thermophilus HB8 in Esm-State at Reaction Time of 6 Min within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn202

b:12.1
occ:0.35
 O A:HOH339 1.9 15.3 1.0
OE2 A:GLU86 2.0 17.6 1.0
O2B A:AR6201 2.1 13.8 0.8
O2A A:AR6201 2.2 22.1 0.8
O A:HOH340 2.3 27.5 1.0
O A:ALA66 2.5 14.1 1.0
O A:HOH394 2.8 8.8 0.2
CD A:GLU86 3.2 13.4 1.0
PB A:AR6201 3.3 12.2 0.8
O3A A:AR6201 3.6 12.9 0.8
C A:ALA66 3.6 9.5 1.0
PA A:AR6201 3.6 17.4 0.8
OE1 A:GLU86 3.6 15.7 1.0
NE2 A:GLN52 3.9 13.4 0.3
OE1 A:GLU82 4.1 12.0 0.3
CA A:GLY67 4.2 12.4 1.0
O1B A:AR6201 4.3 14.3 0.8
O A:HOH312 4.3 11.2 1.0
NH2 A:ARG54 4.4 11.1 1.0
N A:GLY67 4.4 10.0 1.0
NE2 A:GLN52 4.4 18.4 0.7
O5D A:AR6201 4.4 12.4 0.8
CG A:GLU86 4.4 11.6 1.0
OE1 A:GLN52 4.4 25.9 0.7
C5D A:AR6201 4.5 12.1 0.8
O5' A:AR6201 4.5 27.9 0.8
N A:ALA66 4.5 10.0 1.0
CA A:ALA66 4.6 9.6 1.0
O1A A:AR6201 4.6 16.1 0.8
CD A:GLU82 4.7 12.2 0.3
O A:HOH377 4.8 28.6 1.0
CD A:GLN52 4.8 16.5 0.7
CB A:ALA66 5.0 10.3 1.0
CD A:GLN52 5.0 14.1 0.3
OE2 A:GLU82 5.0 18.0 0.3

Reference:

Y.Furuike, Y.Akita, I.Miyahara, N.Kamiya. Adp-Ribose Pyrophosphatase Reaction in Crystalline State Conducted By Consecutive Binding of Two Manganese(II) Ions As Cofactors Biochemistry V. 55 1801 2016.
ISSN: ISSN 0006-2960
PubMed: 26979298
DOI: 10.1021/ACS.BIOCHEM.5B00886
Page generated: Sat Aug 16 13:21:33 2025

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