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Manganese in PDB 3x0o: Adp Ribose Pyrophosphatase From Thermus Thermophilus HB8 in Esmm-State at Reaction Time of 10 Min

Enzymatic activity of Adp Ribose Pyrophosphatase From Thermus Thermophilus HB8 in Esmm-State at Reaction Time of 10 Min

All present enzymatic activity of Adp Ribose Pyrophosphatase From Thermus Thermophilus HB8 in Esmm-State at Reaction Time of 10 Min:
3.6.1.13;

Protein crystallography data

The structure of Adp Ribose Pyrophosphatase From Thermus Thermophilus HB8 in Esmm-State at Reaction Time of 10 Min, PDB code: 3x0o 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 / 1.09
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 49.735, 49.735, 118.974, 90.00, 90.00, 120.00
R / Rfree (%) 15.4 / n/a

Manganese Binding Sites:

The binding sites of Manganese atom in the Adp Ribose Pyrophosphatase From Thermus Thermophilus HB8 in Esmm-State at Reaction Time of 10 Min (pdb code 3x0o). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Adp Ribose Pyrophosphatase From Thermus Thermophilus HB8 in Esmm-State at Reaction Time of 10 Min, PDB code: 3x0o:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 3x0o

Go back to Manganese Binding Sites List in 3x0o
Manganese binding site 1 out of 2 in the Adp Ribose Pyrophosphatase From Thermus Thermophilus HB8 in Esmm-State at Reaction Time of 10 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 Esmm-State at Reaction Time of 10 Min within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn204

b:7.4
occ:0.35
O A:HOH302 2.0 14.0 1.0
O2B A:AR6201 2.1 11.9 0.8
OE2 A:GLU86 2.1 16.6 1.0
O1A A:AR6201 2.2 15.2 0.8
O A:HOH301 2.3 21.2 1.0
O A:ALA66 2.4 12.4 1.0
O A:HOH421 2.9 10.1 0.2
CD A:GLU86 3.2 11.9 1.0
PB A:AR6201 3.3 10.7 0.8
MN A:MN205 3.4 33.3 0.1
PA A:AR6201 3.5 13.3 0.8
C A:ALA66 3.5 8.6 1.0
O3A A:AR6201 3.6 10.9 0.8
OE1 A:GLU86 3.6 14.7 1.0
NE2 A:GLN52 3.8 9.2 0.2
OE2 A:GLU82 4.1 20.6 0.7
CA A:GLY67 4.2 11.9 1.0
O5' A:AR6201 4.2 18.9 0.8
O A:HOH401 4.3 40.0 1.0
O1B A:AR6201 4.3 12.5 0.8
O A:HOH303 4.3 10.6 1.0
N A:GLY67 4.3 9.1 1.0
NE2 A:GLN52 4.4 15.7 0.8
OE1 A:GLN52 4.4 21.4 0.8
NH2 A:ARG54 4.4 9.5 1.0
O5D A:AR6201 4.4 11.5 0.8
CG A:GLU86 4.4 10.3 1.0
N A:ALA66 4.5 9.3 1.0
C5D A:AR6201 4.5 10.8 0.8
O2A A:AR6201 4.6 13.8 0.8
CA A:ALA66 4.6 8.4 1.0
CD1 A:ILE131 4.7 15.5 0.5
CD A:GLU82 4.8 18.2 0.7
O A:HOH359 4.8 28.4 1.0
CD A:GLN52 4.9 13.3 0.8
CD1 A:ILE131 4.9 26.7 0.5
CD A:GLN52 5.0 10.2 0.2
CB A:ALA66 5.0 9.5 1.0

Manganese binding site 2 out of 2 in 3x0o

Go back to Manganese Binding Sites List in 3x0o
Manganese binding site 2 out of 2 in the Adp Ribose Pyrophosphatase From Thermus Thermophilus HB8 in Esmm-State at Reaction Time of 10 Min


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Adp Ribose Pyrophosphatase From Thermus Thermophilus HB8 in Esmm-State at Reaction Time of 10 Min within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn205

b:33.3
occ:0.10
O A:HOH305 1.9 25.4 1.0
O1A A:AR6201 2.3 15.2 0.8
OE2 A:GLU82 2.5 20.6 0.7
OE2 A:GLU86 2.8 16.6 1.0
O A:HOH410 2.9 44.1 1.0
MN A:MN204 3.4 7.4 0.3
OE1 A:GLU82 3.4 16.9 0.7
O A:HOH401 3.4 40.0 1.0
CD A:GLU82 3.4 18.2 0.7
PA A:AR6201 3.5 13.3 0.8
O A:HOH301 3.7 21.2 1.0
CD A:GLU86 3.8 11.9 1.0
CG A:GLU86 3.8 10.3 1.0
O2A A:AR6201 4.0 13.8 0.8
O5' A:AR6201 4.0 18.9 0.8
O A:ALA66 4.4 12.4 1.0
CD1 A:ILE131 4.5 15.5 0.5
OE1 A:GLU85 4.6 14.7 1.0
O3A A:AR6201 4.8 10.9 0.8
CB A:GLU82 4.8 9.2 0.3
CG A:GLU82 4.8 15.6 0.7
OE1 A:GLU86 4.9 14.7 1.0
O2B A:AR6201 5.0 11.9 0.8

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: Tue Dec 15 04:17:22 2020

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