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Copper in PDB 8af3: Sterol Carrier Protein Artifical Metalloenzyme Incorporating Q111C Mutation Coupled to 2,2'-Bipyridine

Enzymatic activity of Sterol Carrier Protein Artifical Metalloenzyme Incorporating Q111C Mutation Coupled to 2,2'-Bipyridine

All present enzymatic activity of Sterol Carrier Protein Artifical Metalloenzyme Incorporating Q111C Mutation Coupled to 2,2'-Bipyridine:
4.2.1.107; 4.2.1.119;

Protein crystallography data

The structure of Sterol Carrier Protein Artifical Metalloenzyme Incorporating Q111C Mutation Coupled to 2,2'-Bipyridine, PDB code: 8af3 was solved by J.M.Richardson, E.Klemencic, A.G.Jarvis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.68 / 1.52
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 35.16, 51.05, 63.06, 90, 90, 90
R / Rfree (%) 22.7 / 23.9

Copper Binding Sites:

The binding sites of Copper atom in the Sterol Carrier Protein Artifical Metalloenzyme Incorporating Q111C Mutation Coupled to 2,2'-Bipyridine (pdb code 8af3). 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 Sterol Carrier Protein Artifical Metalloenzyme Incorporating Q111C Mutation Coupled to 2,2'-Bipyridine, PDB code: 8af3:

Copper binding site 1 out of 1 in 8af3

Go back to Copper Binding Sites List in 8af3
Copper binding site 1 out of 1 in the Sterol Carrier Protein Artifical Metalloenzyme Incorporating Q111C Mutation Coupled to 2,2'-Bipyridine


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Sterol Carrier Protein Artifical Metalloenzyme Incorporating Q111C Mutation Coupled to 2,2'-Bipyridine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu204

b:104.2
occ:1.00
 N2 A:Q8X111 2.0 92.9 1.0
N3 A:Q8X111 2.1 92.4 1.0
O A:HOH328 2.1 89.8 1.0
C7 A:Q8X111 2.8 91.9 1.0
C9 A:Q8X111 2.8 91.4 1.0
C8 A:Q8X111 3.0 92.9 1.0
C13 A:Q8X111 3.1 90.7 1.0
H11 A:Q8X111 3.2 111.5 1.0
H15 A:Q8X111 3.2 108.8 1.0
HG3 A:GLN108 3.4 110.0 1.0
SD A:MET112 3.6 110.8 1.0
HE22 A:GLN90 3.7 85.6 1.0
HE21 A:GLN108 3.7 105.0 1.0
CE A:MET112 3.9 103.5 1.0
C6 A:Q8X111 4.1 89.6 1.0
C10 A:Q8X111 4.1 90.6 1.0
NE2 A:GLN108 4.2 87.5 1.0
CG A:GLN108 4.3 91.6 1.0
C4 A:Q8X111 4.3 89.4 1.0
C12 A:Q8X111 4.4 91.9 1.0
NE2 A:GLN90 4.4 71.3 1.0
OE1 A:GLN90 4.5 76.7 1.0
CD A:GLN108 4.6 87.8 1.0
HE22 A:GLN108 4.7 105.0 1.0
C5 A:Q8X111 4.7 87.6 1.0
CG A:MET112 4.8 108.9 1.0
C11 A:Q8X111 4.8 92.4 1.0
HG2 A:GLN108 4.8 110.0 1.0
CD A:GLN90 4.8 73.6 1.0
H12 A:Q8X111 4.8 108.8 1.0
H10 A:Q8X111 4.8 107.6 1.0
HB2 A:GLN108 4.9 108.0 1.0

Reference:

E.Klemencic, R.Brewster, H.S.Ali, J.M.Richardson, A.G.Jarvis. Exploring the Design of Copper Artificial Metalloenzymes To Be Published.
Page generated: Mon Jul 14 08:47:15 2025

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