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Copper in PDB 6s07: Structure of Formylglycine-Generating Enzyme at 1.04 A in Complex with Copper and Substrate Reveals An Acidic Pocket For Binding and Acti- Vation of Molecular Oxygen.

Enzymatic activity of Structure of Formylglycine-Generating Enzyme at 1.04 A in Complex with Copper and Substrate Reveals An Acidic Pocket For Binding and Acti- Vation of Molecular Oxygen.

All present enzymatic activity of Structure of Formylglycine-Generating Enzyme at 1.04 A in Complex with Copper and Substrate Reveals An Acidic Pocket For Binding and Acti- Vation of Molecular Oxygen.:
1.8.3.7;

Protein crystallography data

The structure of Structure of Formylglycine-Generating Enzyme at 1.04 A in Complex with Copper and Substrate Reveals An Acidic Pocket For Binding and Acti- Vation of Molecular Oxygen., PDB code: 6s07 was solved by F.Leisinger, D.A.Miarzlou, F.P.Seebeck, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.48 / 1.04
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 58.409, 71.939, 76.733, 90.00, 90.00, 90.00
R / Rfree (%) 17.3 / 18

Other elements in 6s07:

The structure of Structure of Formylglycine-Generating Enzyme at 1.04 A in Complex with Copper and Substrate Reveals An Acidic Pocket For Binding and Acti- Vation of Molecular Oxygen. also contains other interesting chemical elements:

Calcium (Ca) 2 atoms
Chlorine (Cl) 1 atom

Copper Binding Sites:

The binding sites of Copper atom in the Structure of Formylglycine-Generating Enzyme at 1.04 A in Complex with Copper and Substrate Reveals An Acidic Pocket For Binding and Acti- Vation of Molecular Oxygen. (pdb code 6s07). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Structure of Formylglycine-Generating Enzyme at 1.04 A in Complex with Copper and Substrate Reveals An Acidic Pocket For Binding and Acti- Vation of Molecular Oxygen., PDB code: 6s07:

Copper binding site 1 out of 1 in 6s07

Go back to Copper Binding Sites List in 6s07
Copper binding site 1 out of 1 in the Structure of Formylglycine-Generating Enzyme at 1.04 A in Complex with Copper and Substrate Reveals An Acidic Pocket For Binding and Acti- Vation of Molecular Oxygen.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Structure of Formylglycine-Generating Enzyme at 1.04 A in Complex with Copper and Substrate Reveals An Acidic Pocket For Binding and Acti- Vation of Molecular Oxygen. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu401

b:9.0
occ:1.00
 SG C:CYS7 2.2 8.7 1.0
SG A:CYS269 2.2 9.4 1.0
SG A:CYS274 2.3 9.5 1.0
HB2 A:ARG276 2.8 10.7 1.0
HG A:CYS269 2.8 11.2 0.0
HZ2 A:TRP228 2.9 10.7 1.0
HG A:CYS274 3.1 11.4 0.0
HA A:CYS269 3.1 11.2 1.0
HB2 A:CYS274 3.2 10.9 1.0
CB A:CYS274 3.2 9.1 1.0
CB A:CYS269 3.3 10.1 1.0
HB3 A:CYS269 3.3 12.1 1.0
O A:HOH603 3.3 11.0 1.0
HB3 A:CYS274 3.3 10.9 1.0
O C:HOH116 3.5 12.0 1.0
CB C:CYS7 3.5 8.9 1.0
CA A:CYS269 3.7 9.3 1.0
HE1 A:TRP228 3.8 10.0 1.0
H A:ARG276 3.8 11.0 1.0
CZ2 A:TRP228 3.8 8.9 1.0
CB A:ARG276 3.8 8.9 1.0
HD2 A:ARG276 3.9 10.9 1.0
O A:HOH604 4.1 14.7 1.0
HB2 A:CYS269 4.1 12.1 1.0
HH11 A:ARG276 4.1 12.1 1.0
HB3 A:ARG276 4.1 10.7 1.0
HG3 A:ARG276 4.3 11.1 1.0
NE1 A:TRP228 4.4 8.3 1.0
N A:CYS269 4.4 9.3 1.0
H A:HIS270 4.4 12.3 1.0
CE2 A:TRP228 4.4 8.1 1.0
N A:ARG276 4.5 9.2 1.0
HA2 A:GLY265 4.5 9.3 1.0
CG A:ARG276 4.5 9.2 1.0
CA A:ARG276 4.6 8.9 1.0
CA A:CYS274 4.6 10.1 1.0
H A:CYS269 4.6 11.2 1.0
HG A:SER266 4.6 10.9 0.0
H A:SER266 4.7 9.6 1.0
CA C:CYS7 4.7 8.6 1.0
CD A:ARG276 4.7 9.1 1.0
HD2 A:TYR273 4.8 11.8 1.0
H A:CYS274 4.8 11.7 1.0
CH2 A:TRP228 4.8 8.6 1.0
HH2 A:TRP228 4.8 10.3 1.0
C A:CYS269 4.9 9.3 1.0
NH1 A:ARG276 5.0 10.1 1.0
N A:HIS270 5.0 10.3 1.0
C A:ARG276 5.0 9.5 1.0

Reference:

D.A.Miarzlou, F.Leisinger, D.Joss, D.Haussinger, F.P.Seebeck. Structure of Formylglycine-Generating Enzyme in Complex with Copper and A Substrate Reveals An Acidic Pocket For Binding and Activation of Molecular Oxygen. Chem Sci V. 10 7049 2019.
ISSN: ISSN 2041-6520
PubMed: 31588272
DOI: 10.1039/C9SC01723B
Page generated: Mon Jul 14 07:13:12 2025

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