Copper in PDB 6dtk: Heterodimers of Fals Mutant Sod Enzyme

All present enzymatic activity of Heterodimers of Fals Mutant Sod Enzyme:
1.15.1.1;

The structure of Heterodimers of Fals Mutant Sod Enzyme, PDB code: 6dtk was solved by V.A.Streltsov, S.D.Nuttall, K.E.Ganio, B.Roberts, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.57 / 2.00
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	162.699, 201.671, 143.834, 90.00, 90.00, 90.00
R / Rfree (%)	15.6 / 19

The structure of Heterodimers of Fals Mutant Sod Enzyme also contains other interesting chemical elements:

Zinc

(Zn)

10 atoms

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 19;

Binding sites:

The binding sites of Copper atom in the Heterodimers of Fals Mutant Sod Enzyme (pdb code 6dtk). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 19 binding sites of Copper where determined in the Heterodimers of Fals Mutant Sod Enzyme, PDB code: 6dtk:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Copper binding site 1 out of 19 in the Heterodimers of Fals Mutant Sod Enzyme


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Heterodimers of Fals Mutant Sod Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu402 b:37.6 occ:0.50 CU A:CU402 0.0 37.6 0.5 CU A:CU402 0.9 39.2 0.3 NE2 A:HIS48 2.0 33.6 1.0 ND1 A:HIS46 2.0 40.6 1.0 NE2 A:HIS120 2.1 39.1 1.0 NE2 A:HIS63 2.8 56.5 1.0 CD2 A:HIS120 2.8 33.7 1.0 CG A:HIS46 2.8 39.5 1.0 CB A:HIS46 3.0 39.7 1.0 CD2 A:HIS48 3.0 32.7 1.0 CE1 A:HIS48 3.0 33.9 1.0 CE1 A:HIS46 3.2 41.9 1.0 CE1 A:HIS120 3.2 35.4 1.0 CD2 A:HIS63 3.4 54.3 1.0 O A:HOH608 3.6 56.9 1.0 CE1 A:HIS63 3.8 60.0 1.0 CD2 A:HIS46 4.0 41.9 1.0 CG A:HIS120 4.1 34.4 1.0 ND1 A:HIS48 4.1 34.9 1.0 CG A:HIS48 4.1 31.4 1.0 CB A:VAL118 4.1 33.4 1.0 NE2 A:HIS46 4.2 40.4 1.0 CA A:HIS46 4.2 38.1 1.0 ND1 A:HIS120 4.2 36.1 1.0 CG1 A:VAL118 4.2 34.6 1.0 N A:HIS46 4.4 36.3 1.0 CG A:HIS63 4.5 49.3 1.0 ND1 A:HIS63 4.7 56.5 1.0 C A:HIS46 4.7 37.8 1.0 O A:HIS46 4.8 35.7 1.0 CG2 A:VAL118 4.8 30.2 1.0 O A:VAL118 4.8 32.9 1.0

Copper binding site 2 out of 19 in the Heterodimers of Fals Mutant Sod Enzyme


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Heterodimers of Fals Mutant Sod Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu402 b:39.2 occ:0.30 CU A:CU402 0.0 39.2 0.3 CU A:CU402 0.9 37.6 0.5 NE2 A:HIS120 2.1 39.1 1.0 ND1 A:HIS46 2.1 40.6 1.0 NE2 A:HIS63 2.1 56.5 1.0 NE2 A:HIS48 2.2 33.6 1.0 O A:HOH608 2.7 56.9 1.0 CE1 A:HIS48 2.8 33.9 1.0 CD2 A:HIS63 2.9 54.3 1.0 CE1 A:HIS120 3.0 35.4 1.0 CE1 A:HIS46 3.1 41.9 1.0 CD2 A:HIS120 3.1 33.7 1.0 CG A:HIS46 3.2 39.5 1.0 CE1 A:HIS63 3.2 60.0 1.0 CD2 A:HIS48 3.3 32.7 1.0 CB A:HIS46 3.5 39.7 1.0 ND1 A:HIS48 4.0 34.9 1.0 CG A:HIS63 4.1 49.3 1.0 ND1 A:HIS120 4.1 36.1 1.0 CG A:HIS120 4.2 34.4 1.0 ND1 A:HIS63 4.2 56.5 1.0 NE2 A:HIS46 4.2 40.4 1.0 CD2 A:HIS46 4.3 41.9 1.0 CG A:HIS48 4.3 31.4 1.0 O A:HOH656 4.7 58.9 1.0 CG1 A:VAL118 4.8 34.6 1.0 CA A:HIS46 4.9 38.1 1.0 CB A:VAL118 4.9 33.4 1.0

Copper binding site 3 out of 19 in the Heterodimers of Fals Mutant Sod Enzyme


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Heterodimers of Fals Mutant Sod Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu404 b:31.9 occ:0.85 CU A:CU404 0.0 31.9 0.8 CU A:CU404 1.3 31.9 0.1 NE2 A:HIS217 2.0 24.4 1.0 NE2 A:HIS289 2.1 29.4 1.0 ND1 A:HIS215 2.1 27.2 1.0 CD2 A:HIS289 2.9 26.4 1.0 NE2 A:HIS232 3.0 31.6 1.0 CE1 A:HIS217 3.0 24.0 1.0 CG A:HIS215 3.0 23.6 1.0 CD2 A:HIS217 3.0 24.2 1.0 CB A:HIS215 3.2 23.8 1.0 CE1 A:HIS289 3.2 27.2 1.0 CE1 A:HIS215 3.2 27.4 1.0 O A:HOH619 3.4 39.7 1.0 CD2 A:HIS232 3.5 31.1 1.0 O A:HOH567 3.6 67.6 1.0 CE1 A:HIS232 3.9 30.9 1.0 CB A:VAL287 4.0 26.4 1.0 ND1 A:HIS217 4.1 25.5 1.0 CG A:HIS289 4.1 26.8 1.0 CG A:HIS217 4.2 24.1 1.0 CD2 A:HIS215 4.2 22.7 1.0 CG1 A:VAL287 4.2 27.2 1.0 CA A:HIS215 4.2 24.1 1.0 ND1 A:HIS289 4.2 26.0 1.0 NE2 A:HIS215 4.2 24.9 1.0 N A:HIS215 4.3 23.1 1.0 O A:HIS215 4.6 24.3 1.0 CG A:HIS232 4.6 31.0 1.0 O A:VAL287 4.6 25.5 1.0 C A:HIS215 4.6 24.4 1.0 CG2 A:VAL287 4.7 25.8 1.0 ND1 A:HIS232 4.8 28.9 1.0

Copper binding site 4 out of 19 in the Heterodimers of Fals Mutant Sod Enzyme


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Heterodimers of Fals Mutant Sod Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu404 b:31.9 occ:0.15 CU A:CU404 0.0 31.9 0.1 CU A:CU404 1.3 31.9 0.8 ND1 A:HIS215 2.0 27.2 1.0 NE2 A:HIS232 2.1 31.6 1.0 NE2 A:HIS289 2.1 29.4 1.0 O A:HOH567 2.3 67.6 1.0 O A:HOH619 2.5 39.7 1.0 CE1 A:HIS215 2.7 27.4 1.0 NE2 A:HIS217 2.8 24.4 1.0 CE1 A:HIS289 3.0 27.2 1.0 CE1 A:HIS232 3.1 30.9 1.0 CD2 A:HIS232 3.1 31.1 1.0 CD2 A:HIS289 3.1 26.4 1.0 CG A:HIS215 3.2 23.6 1.0 CE1 A:HIS217 3.3 24.0 1.0 CB A:HIS215 3.8 23.8 1.0 NE2 A:HIS215 3.9 24.9 1.0 ND1 A:HIS289 4.0 26.0 1.0 CD2 A:HIS217 4.0 24.2 1.0 CG A:HIS289 4.1 26.8 1.0 ND1 A:HIS232 4.1 28.9 1.0 CG A:HIS232 4.2 31.0 1.0 CD2 A:HIS215 4.2 22.7 1.0 O A:HOH555 4.5 45.8 1.0 ND1 A:HIS217 4.6 25.5 1.0 O A:THR306 4.6 32.5 1.0 CG A:HIS217 4.9 24.1 1.0 CB A:THR306 5.0 32.5 1.0

Copper binding site 5 out of 19 in the Heterodimers of Fals Mutant Sod Enzyme


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of Heterodimers of Fals Mutant Sod Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ C:Cu402 b:49.9 occ:0.75 NE2 C:HIS120 2.0 46.2 1.0 ND1 C:HIS46 2.1 55.3 1.0 NE2 C:HIS48 2.1 56.6 1.0 CD2 C:HIS120 2.7 52.5 1.0 CE1 C:HIS48 3.0 53.3 1.0 O C:HOH522 3.0 80.2 1.0 NE2 C:HIS63 3.0 55.0 1.0 CE1 C:HIS46 3.0 51.9 1.0 CG C:HIS46 3.1 52.0 1.0 CD2 C:HIS48 3.2 53.5 1.0 CE1 C:HIS120 3.2 50.5 1.0 CB C:HIS46 3.4 49.9 1.0 CD2 C:HIS63 3.4 56.1 1.0 O C:HOH614 3.9 65.5 1.0 CG C:HIS120 4.0 49.2 1.0 CE1 C:HIS63 4.0 54.8 1.0 ND1 C:HIS48 4.1 56.3 1.0 NE2 C:HIS46 4.2 52.5 1.0 CG1 C:VAL118 4.2 42.7 1.0 ND1 C:HIS120 4.2 50.5 1.0 CD2 C:HIS46 4.2 50.7 1.0 CB C:VAL118 4.2 42.7 1.0 CG C:HIS48 4.3 54.1 1.0 CA C:HIS46 4.4 45.6 1.0 N C:HIS46 4.4 45.4 1.0 CG C:HIS63 4.5 54.5 1.0 O C:VAL118 4.8 37.9 1.0 ND1 C:HIS63 4.8 52.6 1.0 O C:HIS46 4.8 42.9 1.0 C C:HIS46 4.9 44.1 1.0 CG2 C:VAL118 4.9 43.8 1.0

Copper binding site 6 out of 19 in the Heterodimers of Fals Mutant Sod Enzyme


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of Heterodimers of Fals Mutant Sod Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ C:Cu404 b:32.4 occ:0.60 CU C:CU404 0.0 32.4 0.6 CU C:CU404 1.0 30.7 0.2 NE2 C:HIS289 2.0 31.8 1.0 NE2 C:HIS217 2.0 34.3 1.0 ND1 C:HIS215 2.1 37.1 1.0 CD2 C:HIS289 2.8 33.1 1.0 CD2 C:HIS217 2.9 35.4 1.0 CG C:HIS215 2.9 37.8 1.0 NE2 C:HIS232 3.0 42.1 1.0 CB C:HIS215 3.0 35.8 1.0 CE1 C:HIS217 3.1 33.6 1.0 CE1 C:HIS289 3.1 33.9 1.0 CE1 C:HIS215 3.2 36.4 1.0 CD2 C:HIS232 3.4 41.4 1.0 O C:HOH565 3.6 51.7 1.0 CB C:VAL287 4.0 33.3 1.0 CG C:HIS289 4.0 32.0 1.0 CG1 C:VAL287 4.1 33.0 1.0 CE1 C:HIS232 4.1 39.3 1.0 CG C:HIS217 4.1 35.7 1.0 CA C:HIS215 4.1 33.6 1.0 CD2 C:HIS215 4.1 39.0 1.0 ND1 C:HIS289 4.1 31.2 1.0 ND1 C:HIS217 4.1 35.5 1.0 N C:HIS215 4.2 32.4 1.0 NE2 C:HIS215 4.2 37.9 1.0 O C:HIS215 4.6 33.4 1.0 O C:VAL287 4.6 33.3 1.0 C C:HIS215 4.6 33.7 1.0 CG C:HIS232 4.6 37.6 1.0 CG2 C:VAL287 4.7 35.1 1.0 ND1 C:HIS232 4.9 39.0 1.0 C C:VAL287 5.0 33.9 1.0

Copper binding site 7 out of 19 in the Heterodimers of Fals Mutant Sod Enzyme


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 7 of Heterodimers of Fals Mutant Sod Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ C:Cu404 b:30.7 occ:0.20 CU C:CU404 0.0 30.7 0.2 CU C:CU404 1.0 32.4 0.6 ND1 C:HIS215 2.1 37.1 1.0 NE2 C:HIS232 2.1 42.1 1.0 NE2 C:HIS289 2.1 31.8 1.0 NE2 C:HIS217 2.2 34.3 1.0 O C:HOH565 2.7 51.7 1.0 CD2 C:HIS232 2.8 41.4 1.0 CE1 C:HIS217 2.9 33.6 1.0 CE1 C:HIS215 3.0 36.4 1.0 CE1 C:HIS289 3.0 33.9 1.0 CG C:HIS215 3.1 37.8 1.0 CD2 C:HIS289 3.2 33.1 1.0 CE1 C:HIS232 3.3 39.3 1.0 CD2 C:HIS217 3.3 35.4 1.0 CB C:HIS215 3.5 35.8 1.0 CG C:HIS232 4.0 37.6 1.0 ND1 C:HIS289 4.1 31.2 1.0 NE2 C:HIS215 4.1 37.9 1.0 ND1 C:HIS217 4.1 35.5 1.0 CD2 C:HIS215 4.2 39.0 1.0 ND1 C:HIS232 4.2 39.0 1.0 CG C:HIS289 4.2 32.0 1.0 CG C:HIS217 4.3 35.7 1.0 O C:HOH533 4.7 57.2 1.0 CA C:HIS215 4.8 33.6 1.0 O C:HOH620 4.8 56.4 1.0 CG1 C:VAL287 4.8 33.0 1.0 CB C:VAL287 4.9 33.3 1.0 O C:HOH593 5.0 52.2 1.0 N C:HIS215 5.0 32.4 1.0

Copper binding site 8 out of 19 in the Heterodimers of Fals Mutant Sod Enzyme


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 8 of Heterodimers of Fals Mutant Sod Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ E:Cu402 b:28.5 occ:0.60 CU E:CU402 0.0 28.5 0.6 CU E:CU402 1.1 25.6 0.3 NE2 E:HIS120 2.0 26.0 1.0 NE2 E:HIS48 2.0 25.0 1.0 ND1 E:HIS46 2.1 30.1 1.0 CD2 E:HIS120 2.7 26.1 1.0 CG E:HIS46 2.9 28.5 1.0 CD2 E:HIS48 2.9 24.3 1.0 NE2 E:HIS63 3.0 38.0 1.0 CB E:HIS46 3.1 27.0 1.0 CE1 E:HIS48 3.1 25.7 1.0 CE1 E:HIS46 3.1 32.6 1.0 CE1 E:HIS120 3.2 24.5 1.0 O E:HOH623 3.5 48.1 1.0 CD2 E:HIS63 3.6 35.7 1.0 CB E:VAL118 4.0 25.3 1.0 CG E:HIS120 4.0 24.8 1.0 CG1 E:VAL118 4.0 25.7 1.0 CE1 E:HIS63 4.0 33.9 1.0 CD2 E:HIS46 4.1 32.2 1.0 CG E:HIS48 4.1 24.2 1.0 CA E:HIS46 4.2 23.7 1.0 ND1 E:HIS120 4.2 25.1 1.0 ND1 E:HIS48 4.2 25.0 1.0 NE2 E:HIS46 4.2 29.3 1.0 N E:HIS46 4.2 21.5 1.0 O E:HIS46 4.6 22.3 1.0 O E:VAL118 4.6 22.7 1.0 C E:HIS46 4.6 23.2 1.0 CG E:HIS63 4.7 33.8 1.0 CG2 E:VAL118 4.7 25.1 1.0 ND1 E:HIS63 4.9 33.1 1.0

Copper binding site 9 out of 19 in the Heterodimers of Fals Mutant Sod Enzyme


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 9 of Heterodimers of Fals Mutant Sod Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ E:Cu402 b:25.6 occ:0.30 CU E:CU402 0.0 25.6 0.3 CU E:CU402 1.1 28.5 0.6 ND1 E:HIS46 2.1 30.1 1.0 NE2 E:HIS63 2.1 38.0 1.0 NE2 E:HIS48 2.2 25.0 1.0 NE2 E:HIS120 2.2 26.0 1.0 O E:HOH623 2.5 48.1 1.0 CD2 E:HIS63 2.9 35.7 1.0 CE1 E:HIS48 2.9 25.7 1.0 CE1 E:HIS46 3.0 32.6 1.0 CE1 E:HIS120 3.1 24.5 1.0 CD2 E:HIS120 3.1 26.1 1.0 CG E:HIS46 3.2 28.5 1.0 CE1 E:HIS63 3.3 33.9 1.0 CD2 E:HIS48 3.3 24.3 1.0 CB E:HIS46 3.6 27.0 1.0 CG E:HIS63 4.0 33.8 1.0 ND1 E:HIS48 4.1 25.0 1.0 NE2 E:HIS46 4.2 29.3 1.0 ND1 E:HIS120 4.2 25.1 1.0 ND1 E:HIS63 4.2 33.1 1.0 CG E:HIS120 4.2 24.8 1.0 CD2 E:HIS46 4.3 32.2 1.0 CG E:HIS48 4.3 24.2 1.0 O E:HOH785 4.5 43.6 1.0 CG1 E:VAL118 4.8 25.7 1.0 O E:HOH733 4.9 47.1 1.0 CA E:HIS46 4.9 23.7 1.0 CB E:VAL118 4.9 25.3 1.0

Copper binding site 10 out of 19 in the Heterodimers of Fals Mutant Sod Enzyme


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 10 of Heterodimers of Fals Mutant Sod Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ E:Cu404 b:23.1 occ:0.70 CU E:CU404 0.0 23.1 0.7 CU E:CU404 1.1 21.0 0.3 NE2 E:HIS217 2.0 20.3 1.0 NE2 E:HIS289 2.0 21.6 1.0 ND1 E:HIS215 2.1 21.9 1.0 CD2 E:HIS289 2.8 20.6 1.0 CD2 E:HIS217 2.9 18.6 1.0 CG E:HIS215 3.0 20.4 1.0 CE1 E:HIS217 3.1 20.4 1.0 NE2 E:HIS232 3.1 26.0 1.0 CE1 E:HIS289 3.1 22.7 1.0 CB E:HIS215 3.2 20.1 1.0 CE1 E:HIS215 3.2 23.7 1.0 O E:HOH575 3.3 61.6 1.0 O E:HOH662 3.6 37.8 1.0 CD2 E:HIS232 3.6 25.0 1.0 CB E:VAL287 3.9 19.8 1.0 CG E:HIS289 4.0 20.1 1.0 CG E:HIS217 4.1 19.3 1.0 CG1 E:VAL287 4.1 19.6 1.0 CE1 E:HIS232 4.1 24.3 1.0 ND1 E:HIS217 4.1 18.9 1.0 ND1 E:HIS289 4.2 20.6 1.0 CD2 E:HIS215 4.2 21.4 1.0 CA E:HIS215 4.2 19.3 1.0 N E:HIS215 4.2 18.3 1.0 NE2 E:HIS215 4.3 21.1 1.0 O E:HIS215 4.5 19.4 1.0 O E:VAL287 4.5 17.9 1.0 C E:HIS215 4.6 18.9 1.0 CG2 E:VAL287 4.6 20.1 1.0 CG E:HIS232 4.7 23.7 1.0 C E:VAL287 4.9 18.6 1.0 CA E:VAL287 4.9 18.0 1.0 ND1 E:HIS232 4.9 23.7 1.0

V.A.Streltsov, S.D.Nuttall, K.E.Ganio, B.Roberts. Structural Characterization of Heterodimers of Fals Mutant Sod Enzyme To Be Published.