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Copper in PDB 6nfq: Copc From Pseudomonas Fluorescens

Protein crystallography data

The structure of Copc From Pseudomonas Fluorescens, PDB code: 6nfq was solved by M.J.Maher, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.00 / 2.00
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 77.730, 111.319, 82.222, 90.00, 90.00, 90.00
R / Rfree (%) 22.8 / 26

Other elements in 6nfq:

The structure of Copc From Pseudomonas Fluorescens also contains other interesting chemical elements:

Yttrium (Y) 1 atom

Copper Binding Sites:

The binding sites of Copper atom in the Copc From Pseudomonas Fluorescens (pdb code 6nfq). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the Copc From Pseudomonas Fluorescens, PDB code: 6nfq:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in 6nfq

Go back to Copper Binding Sites List in 6nfq
Copper binding site 1 out of 3 in the Copc From Pseudomonas Fluorescens


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Copc From Pseudomonas Fluorescens within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu201

b:19.4
occ:1.00
ND1 A:HIS109 1.8 55.5 1.0
N A:HIS25 2.2 52.0 1.0
ND1 A:HIS25 2.3 52.8 1.0
OD2 A:ASP107 2.6 56.1 1.0
CG A:HIS109 2.8 55.6 1.0
CE1 A:HIS109 2.8 59.1 1.0
CA A:HIS25 3.0 46.6 1.0
CG A:HIS25 3.1 50.3 1.0
CE1 A:HIS25 3.1 50.6 1.0
CB A:HIS109 3.2 50.5 1.0
CG A:ASP107 3.3 54.9 1.0
OD1 A:ASP107 3.4 62.0 1.0
CB A:HIS25 3.4 47.0 1.0
NE2 A:HIS109 3.9 60.3 1.0
CD2 A:HIS109 3.9 58.5 1.0
NE2 A:HIS25 4.0 53.4 1.0
CD2 A:HIS25 4.0 50.4 1.0
C A:HIS25 4.4 40.6 1.0
CA A:HIS109 4.6 46.3 1.0
OE1 A:GLU51 4.7 57.4 1.0
OE2 A:GLU51 4.8 59.4 1.0
CB A:ASP107 4.8 55.5 1.0
OG A:SER105 4.9 56.8 1.0
O A:HIS25 4.9 43.1 1.0
N A:HIS109 5.0 45.5 1.0

Copper binding site 2 out of 3 in 6nfq

Go back to Copper Binding Sites List in 6nfq
Copper binding site 2 out of 3 in the Copc From Pseudomonas Fluorescens


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Copc From Pseudomonas Fluorescens within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu201

b:15.5
occ:1.00
ND1 B:HIS109 2.1 41.1 1.0
OD2 B:ASP107 2.1 49.5 1.0
N B:HIS25 2.1 39.1 1.0
ND1 B:HIS25 2.3 44.6 1.0
CG B:HIS109 2.9 36.3 1.0
CA B:HIS25 3.0 39.9 1.0
CE1 B:HIS25 3.0 49.0 1.0
CB B:HIS109 3.0 31.0 1.0
CG B:HIS25 3.1 46.7 1.0
CE1 B:HIS109 3.2 38.3 1.0
CG B:ASP107 3.3 47.0 1.0
CB B:HIS25 3.5 46.3 1.0
NE2 B:HIS25 3.9 46.0 1.0
CD2 B:HIS25 3.9 46.3 1.0
CB B:ASP107 4.0 44.2 1.0
CD2 B:HIS109 4.1 37.6 1.0
NE2 B:HIS109 4.2 38.9 1.0
OE1 B:GLU51 4.2 38.8 1.0
OD1 B:ASP107 4.2 68.4 1.0
C B:HIS25 4.4 40.5 1.0
CA B:HIS109 4.5 31.9 1.0
N B:HIS109 4.9 28.9 1.0
O B:HIS25 4.9 38.3 1.0

Copper binding site 3 out of 3 in 6nfq

Go back to Copper Binding Sites List in 6nfq
Copper binding site 3 out of 3 in the Copc From Pseudomonas Fluorescens


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Copc From Pseudomonas Fluorescens within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu201

b:15.2
occ:1.00
ND1 C:HIS25 1.9 43.2 1.0
N C:HIS25 2.2 43.6 1.0
ND1 C:HIS109 2.3 45.5 1.0
OD2 C:ASP107 2.4 42.8 1.0
CE1 C:HIS25 2.7 51.2 1.0
CG C:HIS109 2.9 42.0 1.0
CG C:HIS25 3.0 43.9 1.0
CB C:HIS109 3.1 38.8 1.0
CA C:HIS25 3.1 37.6 1.0
CE1 C:HIS109 3.3 49.5 1.0
CG C:ASP107 3.3 46.8 1.0
CB C:HIS25 3.4 37.2 1.0
OD1 C:ASP107 3.5 40.7 1.0
NE2 C:HIS25 3.9 52.0 1.0
CD2 C:HIS25 4.0 43.3 1.0
CD2 C:HIS109 4.0 46.2 1.0
NE2 C:HIS109 4.2 49.3 1.0
C C:HIS25 4.5 36.5 1.0
CA C:HIS109 4.5 39.6 1.0
OE2 C:GLU51 4.5 51.7 1.0
CB C:ASP107 4.7 42.2 1.0
N C:HIS109 4.9 41.1 1.0

Reference:

S.R.Udagedara, C.J.K.Wijekoon, Z.Xiao, A.G.Wedd, M.J.Maher. The Crystal Structure of the Copc Protein From Pseudomonas Fluorescens Reveals Amended Classifications For the Copc Protein Family. J. Inorg. Biochem. V. 195 194 2019.
ISSN: ISSN 1873-3344
PubMed: 30981030
DOI: 10.1016/J.JINORGBIO.2019.03.007
Page generated: Mon Jul 14 06:34:15 2025

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