Atomistry » Copper » PDB 5i26-5luf » 5kbl
Atomistry »
  Copper »
    PDB 5i26-5luf »
      5kbl »

Copper in PDB 5kbl: Candida Albicans Superoxide Dismutase 5 (SOD5), E110Q Mutant

Enzymatic activity of Candida Albicans Superoxide Dismutase 5 (SOD5), E110Q Mutant

All present enzymatic activity of Candida Albicans Superoxide Dismutase 5 (SOD5), E110Q Mutant:
1.15.1.1;

Protein crystallography data

The structure of Candida Albicans Superoxide Dismutase 5 (SOD5), E110Q Mutant, PDB code: 5kbl was solved by A.Galaleldeen, R.L.Peterson, J.Villarreal, A.B.Taylor, P.J.Hart, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.53 / 1.41
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 34.364, 40.349, 102.257, 90.00, 90.00, 90.00
R / Rfree (%) 15.6 / 20.4

Copper Binding Sites:

The binding sites of Copper atom in the Candida Albicans Superoxide Dismutase 5 (SOD5), E110Q Mutant (pdb code 5kbl). 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 Candida Albicans Superoxide Dismutase 5 (SOD5), E110Q Mutant, PDB code: 5kbl:

Copper binding site 1 out of 1 in 5kbl

Go back to Copper Binding Sites List in 5kbl
Copper binding site 1 out of 1 in the Candida Albicans Superoxide Dismutase 5 (SOD5), E110Q Mutant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Candida Albicans Superoxide Dismutase 5 (SOD5), E110Q Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu201

b:16.9
occ:0.90
NE2 A:HIS77 2.0 13.5 1.0
NE2 A:HIS153 2.0 15.5 1.0
ND1 A:HIS75 2.0 14.9 1.0
CE1 A:HIS77 2.9 14.3 1.0
CD2 A:HIS153 2.9 16.1 1.0
CE1 A:HIS75 3.0 16.0 1.0
CD2 A:HIS77 3.0 13.4 1.0
CG A:HIS75 3.1 14.9 1.0
CE1 A:HIS153 3.1 16.1 1.0
NE2 A:HIS93 3.3 24.0 1.0
CB A:HIS75 3.4 12.4 1.0
O A:HOH363 3.5 33.3 1.0
CD2 A:HIS93 3.8 23.0 1.0
CB A:VAL151 3.9 11.0 1.0
O A:VAL151 4.0 11.5 1.0
N A:HIS75 4.0 12.0 1.0
ND1 A:HIS77 4.0 13.1 1.0
CG A:HIS153 4.1 15.3 1.0
ND1 A:HIS153 4.1 15.2 1.0
NE2 A:HIS75 4.1 15.5 1.0
CG A:HIS77 4.1 12.4 1.0
CD2 A:HIS75 4.2 13.9 1.0
CA A:HIS75 4.2 11.7 1.0
CE1 A:HIS93 4.2 23.7 1.0
CG1 A:VAL151 4.3 13.1 1.0
O A:HIS75 4.4 11.4 1.0
C A:VAL151 4.6 12.4 1.0
C A:HIS75 4.6 12.2 1.0
CA A:VAL151 4.8 10.7 1.0
CG2 A:VAL151 4.8 11.8 1.0
C A:TYR74 4.8 12.0 1.0
CG A:HIS93 4.8 21.5 1.0
ND1 A:HIS93 5.0 21.6 1.0
N A:VAL151 5.0 10.7 1.0

Reference:

R.L.Peterson, A.Galaleldeen, J.Villarreal, A.B.Taylor, D.E.Cabelli, P.J.Hart, V.C.Culotta. The Phylogeny and Active Site Design of Eukaryotic Copper-Only Superoxide Dismutases. J.Biol.Chem. V. 291 20911 2016.
ISSN: ESSN 1083-351X
PubMed: 27535222
DOI: 10.1074/JBC.M116.748251
Page generated: Sun Dec 13 11:18:17 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