Atomistry » Manganese » PDB 3ebc-3g0a » 3ee4
Atomistry »
  Manganese »
    PDB 3ebc-3g0a »
      3ee4 »

Manganese in PDB 3ee4: R2-Like Ligand Binding Mn/Fe Oxidase From M. Tuberculosis

Enzymatic activity of R2-Like Ligand Binding Mn/Fe Oxidase From M. Tuberculosis

All present enzymatic activity of R2-Like Ligand Binding Mn/Fe Oxidase From M. Tuberculosis:
1.17.4.1;

Protein crystallography data

The structure of R2-Like Ligand Binding Mn/Fe Oxidase From M. Tuberculosis, PDB code: 3ee4 was solved by C.S.Andersson, T.A.Jones, M.Hogbom, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.85 / 1.90
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 54.565, 54.565, 176.651, 90.00, 90.00, 120.00
R / Rfree (%) 14.9 / 17.7

Other elements in 3ee4:

The structure of R2-Like Ligand Binding Mn/Fe Oxidase From M. Tuberculosis also contains other interesting chemical elements:

Iron (Fe) 1 atom

Manganese Binding Sites:

The binding sites of Manganese atom in the R2-Like Ligand Binding Mn/Fe Oxidase From M. Tuberculosis (pdb code 3ee4). 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 R2-Like Ligand Binding Mn/Fe Oxidase From M. Tuberculosis, PDB code: 3ee4:

Manganese binding site 1 out of 1 in 3ee4

Go back to Manganese Binding Sites List in 3ee4
Manganese binding site 1 out of 1 in the R2-Like Ligand Binding Mn/Fe Oxidase From M. Tuberculosis


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of R2-Like Ligand Binding Mn/Fe Oxidase From M. Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn316

b:15.6
occ:1.00
OE1 A:GLU101 2.0 16.6 1.0
OE1 A:GLU68 2.0 14.0 1.0
O2 A:MYR315 2.0 27.9 1.0
O A:HOH343 2.2 16.2 1.0
ND1 A:HIS104 2.2 8.1 1.0
O A:HOH483 3.0 42.3 1.0
CD A:GLU68 3.0 18.4 1.0
CD A:GLU101 3.1 16.0 1.0
CE1 A:HIS104 3.1 10.6 1.0
C1 A:MYR315 3.1 25.9 1.0
OE2 A:GLU68 3.3 19.9 1.0
CG A:HIS104 3.3 11.9 1.0
O1 A:MYR315 3.4 22.3 1.0
OE2 A:GLU101 3.5 16.4 1.0
FE A:FE317 3.6 19.9 1.0
CB A:HIS104 3.8 11.9 1.0
OE2 A:GLU202 4.0 34.8 1.0
OE1 A:GLU202 4.2 22.8 1.0
NE2 A:HIS104 4.3 13.3 1.0
CG A:GLU68 4.3 13.7 1.0
CG2 A:ILE198 4.3 24.2 1.0
CG A:GLU101 4.4 14.2 1.0
C2 A:MYR315 4.4 21.9 1.0
CD2 A:HIS104 4.4 9.0 1.0
CA A:GLU101 4.5 10.6 1.0
CD A:GLU202 4.5 32.8 1.0
CG2 A:VAL71 4.7 12.8 1.0
C3 A:MYR315 4.7 22.2 1.0
CB A:GLU101 4.7 11.0 1.0
CE1 A:HIS205 4.7 11.1 1.0
CB A:GLU68 4.8 12.0 1.0
ND1 A:HIS205 4.8 13.6 1.0
OH A:TYR175 4.9 17.3 1.0

Reference:

C.S.Andersson, C.S.Andersson, T.A.Jones, M.Hogbom. N/A N/A.
ISSN: ISSN 0027-8424
PubMed: 19321420
DOI: 10.1073/PNAS.0812971106
Page generated: Tue Dec 15 04:09:08 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy