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Manganese in PDB 3rvo: Structure of Chey-MN2+ Complex with Substitutions at 59 and 89: N59D E89Y

Protein crystallography data

The structure of Structure of Chey-MN2+ Complex with Substitutions at 59 and 89: N59D E89Y, PDB code: 3rvo was solved by R.M.Immormino, C.A.Starbird, R.E.Silversmith, R.B.Bourret, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 23.44 / 1.55
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 45.364, 46.885, 53.524, 90.00, 90.00, 90.00
R / Rfree (%) 15.2 / 18.5

Manganese Binding Sites:

The binding sites of Manganese atom in the Structure of Chey-MN2+ Complex with Substitutions at 59 and 89: N59D E89Y (pdb code 3rvo). 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 Structure of Chey-MN2+ Complex with Substitutions at 59 and 89: N59D E89Y, PDB code: 3rvo:

Manganese binding site 1 out of 1 in 3rvo

Go back to Manganese Binding Sites List in 3rvo
Manganese binding site 1 out of 1 in the Structure of Chey-MN2+ Complex with Substitutions at 59 and 89: N59D E89Y


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of Chey-MN2+ Complex with Substitutions at 59 and 89: N59D E89Y within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn130

b:12.6
occ:0.82
OD2 A:ASP57 2.2 11.9 0.5
O A:ASP59 2.3 10.7 1.0
O A:HOH137 2.3 22.6 1.0
OD1 A:ASP13 2.3 13.1 1.0
OD2 A:ASP57 2.3 13.9 0.5
O A:HOH274 2.3 14.2 1.0
O A:HOH275 2.4 14.3 1.0
CG A:ASP57 3.2 12.0 0.5
CG A:ASP13 3.4 14.9 1.0
OD1 A:ASP57 3.5 15.7 0.5
C A:ASP59 3.5 10.2 1.0
CG A:ASP57 3.6 14.3 0.5
HB3 A:ASP59 3.6 13.9 1.0
HG2 A:MET60 3.7 8.6 1.0
HD1 A:PHE14 3.7 18.6 0.4
H A:ASP13 3.8 12.0 1.0
OD2 A:ASP13 3.8 14.3 1.0
HA A:MET60 3.8 8.4 1.0
OD2 A:ASP12 4.0 11.6 1.0
HE1 A:PHE14 4.1 19.2 0.4
HZ1 A:LYS109 4.2 27.4 0.5
H A:ASP59 4.2 10.9 1.0
O A:HOH249 4.2 23.8 1.0
HB3 A:ASP57 4.3 9.2 0.5
OD1 A:ASP57 4.3 14.9 0.5
CD1 A:PHE14 4.3 15.6 0.4
HG3 A:MET60 4.4 8.6 1.0
CB A:ASP59 4.4 11.6 1.0
CA A:ASP59 4.4 10.5 1.0
CG A:MET60 4.4 7.2 1.0
O A:HOH177 4.4 21.8 0.5
N A:MET60 4.5 8.1 1.0
CB A:ASP57 4.5 8.9 0.5
CB A:ASP57 4.5 7.7 0.5
CA A:MET60 4.5 7.0 1.0
CE1 A:PHE14 4.6 16.0 0.4
O A:HOH153 4.6 11.4 1.0
N A:ASP13 4.6 10.0 1.0
HB3 A:ASP57 4.6 10.7 0.5
O A:HOH278 4.6 33.4 1.0
N A:ASP59 4.7 9.1 1.0
CG A:ASP12 4.7 14.0 1.0
CB A:ASP13 4.7 14.3 1.0
HB2 A:ASP57 4.8 10.7 0.5
CE2 A:PHE14 4.8 16.3 0.6
H A:PHE14 4.8 13.8 0.6
H A:PHE14 4.8 13.8 0.4
CG A:ASP59 4.9 15.4 1.0
CZ A:PHE14 4.9 16.3 0.6
HB2 A:ASP57 4.9 9.2 0.5
OD1 A:ASP12 4.9 14.2 1.0
CD2 A:PHE14 4.9 15.9 0.6
HB3 A:ASP13 4.9 17.2 1.0
HA A:ASP12 4.9 9.8 1.0
HE2 A:PHE14 5.0 19.6 0.6
NZ A:LYS109 5.0 22.8 0.5

Reference:

R.M.Immormino, C.A.Starbird, R.E.Silversmith, R.B.Bourret. Probing Mechanistic Similarities Between Response Regulator Signaling Proteins and Haloacid Dehalogenase Phosphatases. Biochemistry V. 54 3514 2015.
ISSN: ISSN 0006-2960
PubMed: 25928369
DOI: 10.1021/ACS.BIOCHEM.5B00286
Page generated: Tue Dec 15 04:15:02 2020

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