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Manganese in PDB 3rvq: Structure of the Chey-MN2+ Complex with Substitutions at 59 and 89: N59D E89K

Protein crystallography data

The structure of Structure of the Chey-MN2+ Complex with Substitutions at 59 and 89: N59D E89K, PDB code: 3rvq 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) 27.37 / 1.15
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 29.723, 43.399, 46.308, 90.00, 103.30, 90.00
R / Rfree (%) 10.9 / 12.5

Manganese Binding Sites:

The binding sites of Manganese atom in the Structure of the Chey-MN2+ Complex with Substitutions at 59 and 89: N59D E89K (pdb code 3rvq). 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 the Chey-MN2+ Complex with Substitutions at 59 and 89: N59D E89K, PDB code: 3rvq:

Manganese binding site 1 out of 1 in 3rvq

Go back to Manganese Binding Sites List in 3rvq
Manganese binding site 1 out of 1 in the Structure of the Chey-MN2+ Complex with Substitutions at 59 and 89: N59D E89K


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of the Chey-MN2+ Complex with Substitutions at 59 and 89: N59D E89K within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn130

b:7.1
occ:1.00
OD2 A:ASP57 2.0 7.6 0.5
O A:ASP59 2.2 6.4 1.0
O A:HOH312 2.3 6.5 0.7
OD1 A:ASP13 2.3 4.8 1.0
O A:HOH291 2.3 3.3 0.8
O A:HOH290 2.3 3.8 0.8
OD2 A:ASP57 2.3 5.8 0.5
OD1 A:ASP57 2.9 6.0 0.5
CG A:ASP57 3.0 5.6 0.5
CG A:ASP57 3.1 6.8 0.5
CG A:ASP13 3.3 4.4 1.0
HG2 A:MET60 3.3 5.9 1.0
C A:ASP59 3.4 6.2 1.0
OD1 A:ASP57 3.6 7.3 0.5
OD2 A:ASP13 3.7 5.0 1.0
HZ1 A:LYS109 3.7 6.4 1.0
HA A:MET60 3.7 6.9 1.0
HB3 A:ASP59 3.7 11.1 1.0
H A:ASP13 3.8 4.4 1.0
HG3 A:MET60 4.0 5.9 1.0
CG A:MET60 4.1 4.9 1.0
OD1 A:ASP12 4.2 5.1 1.0
O A:HOH302 4.2 4.3 0.6
HB3 A:ASP57 4.3 6.5 0.5
N A:MET60 4.3 6.0 1.0
H A:ASP59 4.3 7.5 1.0
CA A:ASP59 4.3 7.3 1.0
O A:HOH152 4.4 16.3 1.0
CA A:MET60 4.4 5.8 1.0
CB A:ASP57 4.4 5.5 0.5
O A:HOH295 4.4 4.2 0.7
CB A:ASP57 4.5 4.9 0.5
CB A:ASP59 4.5 9.3 1.0
NZ A:LYS109 4.5 5.3 1.0
N A:ASP59 4.5 6.3 1.0
HZ3 A:LYS109 4.5 6.4 1.0
N A:ASP13 4.6 3.6 1.0
CB A:ASP13 4.6 4.5 1.0
HD3 A:PRO61 4.8 8.8 1.0
HB3 A:ASP13 4.8 5.4 1.0
HB2 A:ASP57 4.8 6.5 0.5
CG A:ASP12 4.8 4.4 1.0
CB A:MET60 4.8 5.5 1.0
HA A:ASP12 4.9 4.5 1.0
H A:PHE14 4.9 4.7 1.0
O A:HOH236 4.9 10.4 0.7
H A:TRP58 4.9 6.3 1.0
CE2 A:PHE14 5.0 6.8 1.0

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: Sat Oct 5 17:51:26 2024

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