Atomistry » Silver » PDB 1aoo-6ka0 » 5nxl
Atomistry »
  Silver »
    PDB 1aoo-6ka0 »
      5nxl »

Silver in PDB 5nxl: Formylglycine Generating Enzyme From T. Curvata in Complex with Ag(I)

Enzymatic activity of Formylglycine Generating Enzyme From T. Curvata in Complex with Ag(I)

All present enzymatic activity of Formylglycine Generating Enzyme From T. Curvata in Complex with Ag(I):
2.7.11.1;

Protein crystallography data

The structure of Formylglycine Generating Enzyme From T. Curvata in Complex with Ag(I), PDB code: 5nxl was solved by M.Meury, M.Knop, F.P.Seebeck, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.63 / 1.66
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 40.947, 65.572, 99.501, 90.00, 90.00, 90.00
R / Rfree (%) 17 / 19.8

Other elements in 5nxl:

The structure of Formylglycine Generating Enzyme From T. Curvata in Complex with Ag(I) also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Silver Binding Sites:

The binding sites of Silver atom in the Formylglycine Generating Enzyme From T. Curvata in Complex with Ag(I) (pdb code 5nxl). This binding sites where shown within 5.0 Angstroms radius around Silver atom.
In total only one binding site of Silver was determined in the Formylglycine Generating Enzyme From T. Curvata in Complex with Ag(I), PDB code: 5nxl:

Silver binding site 1 out of 1 in 5nxl

Go back to Silver Binding Sites List in 5nxl
Silver binding site 1 out of 1 in the Formylglycine Generating Enzyme From T. Curvata in Complex with Ag(I)


Mono view


Stereo pair view

A full contact list of Silver with other atoms in the Ag binding site number 1 of Formylglycine Generating Enzyme From T. Curvata in Complex with Ag(I) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ag401

b:15.8
occ:1.00
 SG A:CYS274 2.3 16.9 1.0
SG A:CYS269 2.3 13.9 1.0
O A:CYS274 3.1 15.8 1.0
CB A:CYS274 3.2 13.1 1.0
CB A:CYS269 3.3 13.3 1.0
C A:CYS274 3.6 15.8 1.0
O A:HOH562 3.6 13.0 1.0
N A:ARG276 3.6 13.6 1.0
CA A:CYS269 3.7 14.3 1.0
CB A:ARG276 3.9 13.8 1.0
CZ2 A:TRP228 3.9 17.6 1.0
CA A:CYS274 4.0 12.7 1.0
O A:HOH691 4.1 38.0 1.0
CA A:ARG276 4.2 11.3 1.0
O A:HOH608 4.3 23.0 1.0
N A:ASN275 4.3 16.9 1.0
CG A:ARG276 4.4 17.7 1.0
N A:CYS269 4.6 13.8 1.0
C A:ASN275 4.6 15.6 1.0
CA A:GLY265 4.7 14.9 1.0
C A:ARG276 4.7 16.1 1.0
CH2 A:TRP228 4.7 17.2 1.0
CE2 A:TRP228 4.7 13.6 1.0
N A:TYR277 4.8 16.9 1.0
CA A:ASN275 4.8 13.4 1.0
C A:CYS269 4.8 15.9 1.0
NE1 A:TRP228 4.8 15.5 1.0
N A:HIS270 4.9 14.1 1.0

Reference:

M.Meury, M.Knop, F.P.Seebeck. Structural Basis For Copper-Oxygen Mediated C-H Bond Activation By the Formylglycine-Generating Enzyme. Angew. Chem. Int. Ed. Engl. V. 56 8115 2017.
ISSN: ESSN 1521-3773
PubMed: 28544744
DOI: 10.1002/ANIE.201702901
Page generated: Sat Dec 12 01:22:29 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