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Copper in PDB 3nq5: Crystal Structure of Tyrosinase From Bacillus Megaterium R209H Mutant

Enzymatic activity of Crystal Structure of Tyrosinase From Bacillus Megaterium R209H Mutant

All present enzymatic activity of Crystal Structure of Tyrosinase From Bacillus Megaterium R209H Mutant:
1.14.18.1;

Protein crystallography data

The structure of Crystal Structure of Tyrosinase From Bacillus Megaterium R209H Mutant, PDB code: 3nq5 was solved by M.Sendovski, M.Kanteev, N.Adir, A.Fishman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.93 / 2.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 49.130, 80.850, 147.110, 90.00, 90.00, 90.00
R / Rfree (%) 21.7 / 30.4

Other elements in 3nq5:

The structure of Crystal Structure of Tyrosinase From Bacillus Megaterium R209H Mutant also contains other interesting chemical elements:

Zinc (Zn) 10 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Tyrosinase From Bacillus Megaterium R209H Mutant (pdb code 3nq5). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Crystal Structure of Tyrosinase From Bacillus Megaterium R209H Mutant, PDB code: 3nq5:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 3nq5

Go back to Copper Binding Sites List in 3nq5
Copper binding site 1 out of 4 in the Crystal Structure of Tyrosinase From Bacillus Megaterium R209H Mutant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of Tyrosinase From Bacillus Megaterium R209H Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:31.8
occ:1.00
 NE2 A:HIS60 1.9 23.4 1.0
NE2 A:HIS42 2.1 23.2 1.0
CE1 A:HIS42 2.7 22.3 1.0
CE1 A:HIS60 2.8 21.7 1.0
CD2 A:HIS60 3.0 22.0 1.0
O A:HOH380 3.1 33.8 1.0
CD2 A:HIS42 3.4 19.1 1.0
CU A:CU502 3.6 22.3 1.0
NE2 A:HIS69 3.8 19.8 1.0
CE2 A:PHE227 3.8 13.8 1.0
CZ A:PHE227 3.9 16.7 1.0
ND1 A:HIS42 4.0 21.4 1.0
ND1 A:HIS60 4.0 21.5 1.0
CG A:HIS60 4.1 20.1 1.0
CG1 A:VAL218 4.2 29.6 1.0
CG A:HIS42 4.3 18.5 1.0
CE1 A:HIS69 4.4 15.9 1.0
NE2 A:HIS208 4.5 12.7 1.0
O A:VAL218 4.6 33.5 1.0
CA A:VAL218 4.7 30.1 1.0
CG2 A:VAL218 4.7 29.6 1.0
CE1 A:HIS208 4.7 11.7 1.0
CB A:VAL218 4.8 32.3 1.0
NE2 A:HIS231 4.8 14.3 1.0
CB A:ALA221 4.9 14.8 1.0
NE2 A:HIS204 4.9 18.4 1.0

Copper binding site 2 out of 4 in 3nq5

Go back to Copper Binding Sites List in 3nq5
Copper binding site 2 out of 4 in the Crystal Structure of Tyrosinase From Bacillus Megaterium R209H Mutant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of Tyrosinase From Bacillus Megaterium R209H Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu502

b:22.3
occ:1.00
 NE2 A:HIS231 1.9 14.3 1.0
NE2 A:HIS208 1.9 12.7 1.0
NE2 A:HIS204 2.1 18.4 1.0
CE1 A:HIS231 2.7 15.2 1.0
CD2 A:HIS208 2.8 17.6 1.0
CE1 A:HIS208 3.0 11.7 1.0
CE1 A:HIS204 3.0 20.6 1.0
CD2 A:HIS204 3.1 19.7 1.0
CD2 A:HIS231 3.1 11.4 1.0
CE2 A:PHE227 3.5 13.8 1.0
CU A:CU501 3.6 31.8 1.0
O A:HOH380 3.7 33.8 1.0
ND1 A:HIS231 3.9 11.9 1.0
CZ A:PHE227 3.9 16.7 1.0
CG A:HIS208 4.0 16.5 1.0
ND1 A:HIS208 4.0 11.8 1.0
CG A:HIS231 4.1 11.2 1.0
ND1 A:HIS204 4.1 18.9 1.0
CG A:HIS204 4.2 23.6 1.0
NE2 A:HIS69 4.2 19.8 1.0
CD2 A:PHE227 4.4 15.7 1.0
CE1 A:HIS230 4.5 19.4 1.0
CE1 A:PHE65 4.6 19.7 1.0
ND1 A:HIS230 4.6 17.2 1.0
NE2 A:HIS60 4.7 23.4 1.0
CE1 A:HIS69 4.8 15.9 1.0
CD2 A:HIS69 4.8 19.4 1.0

Copper binding site 3 out of 4 in 3nq5

Go back to Copper Binding Sites List in 3nq5
Copper binding site 3 out of 4 in the Crystal Structure of Tyrosinase From Bacillus Megaterium R209H Mutant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Crystal Structure of Tyrosinase From Bacillus Megaterium R209H Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu501

b:28.3
occ:1.00
 NE2 B:HIS42 2.1 16.8 1.0
NE2 B:HIS60 2.3 15.6 1.0
CE1 B:HIS42 2.9 14.6 1.0
O B:HOH393 3.0 13.7 1.0
CE1 B:HIS60 3.1 20.2 1.0
CD2 B:HIS42 3.3 15.6 1.0
CD2 B:HIS60 3.3 17.4 1.0
NE2 B:HIS69 3.6 13.1 1.0
CU B:CU502 3.6 24.1 1.0
CG2 B:VAL218 3.8 17.8 1.0
CG1 B:VAL218 3.9 23.1 1.0
CZ B:PHE227 4.0 15.4 1.0
CE2 B:PHE227 4.1 13.1 1.0
ND1 B:HIS42 4.1 13.2 1.0
ND1 B:HIS60 4.3 16.1 1.0
CG B:HIS42 4.3 14.3 1.0
CB B:VAL218 4.3 22.8 1.0
CE1 B:HIS69 4.3 15.4 1.0
CG B:HIS60 4.4 17.6 1.0
CA B:VAL218 4.6 20.2 1.0
CD2 B:HIS69 4.7 12.5 1.0
NE2 B:HIS208 4.7 22.7 1.0
O B:VAL218 4.7 23.8 1.0
NE2 B:HIS231 4.9 11.4 1.0
CE1 B:HIS208 4.9 18.5 1.0
CB B:ALA221 5.0 15.4 1.0

Copper binding site 4 out of 4 in 3nq5

Go back to Copper Binding Sites List in 3nq5
Copper binding site 4 out of 4 in the Crystal Structure of Tyrosinase From Bacillus Megaterium R209H Mutant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Crystal Structure of Tyrosinase From Bacillus Megaterium R209H Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu502

b:24.1
occ:1.00
 NE2 B:HIS208 2.0 22.7 1.0
NE2 B:HIS231 2.1 11.4 1.0
NE2 B:HIS204 2.1 17.5 1.0
CE1 B:HIS231 2.8 10.2 1.0
CE1 B:HIS208 2.9 18.5 1.0
CE1 B:HIS204 3.0 16.1 1.0
CD2 B:HIS208 3.0 21.7 1.0
CD2 B:HIS204 3.2 14.2 1.0
CD2 B:HIS231 3.3 11.1 1.0
CU B:CU501 3.6 28.3 1.0
O B:HOH393 3.9 13.7 1.0
CE2 B:PHE227 3.9 13.1 1.0
ND1 B:HIS231 4.0 9.8 1.0
CZ B:PHE227 4.0 15.4 1.0
ND1 B:HIS208 4.1 17.9 1.0
CG B:HIS208 4.1 19.1 1.0
ND1 B:HIS204 4.2 16.4 1.0
CG B:HIS204 4.3 16.5 1.0
CG B:HIS231 4.3 10.4 1.0
NE2 B:HIS69 4.3 13.1 1.0
CE1 B:HIS230 4.3 14.0 1.0
ND1 B:HIS230 4.5 14.6 1.0
CD2 B:HIS69 4.6 12.5 1.0
CE1 B:PHE65 4.7 19.1 1.0
CD2 B:PHE227 4.8 13.2 1.0
O B:HOH407 4.9 26.4 1.0
CE1 B:PHE227 4.9 14.9 1.0
NE2 B:HIS60 5.0 15.6 1.0

Reference:

M.Sendovski, M.Kanteev, V.Shuster Ben-Yosef, N.Adir, A.Fishman. First Structures of An Active Bacterial Tyrosinase Reveal Copper Plasticity. J.Mol.Biol. V. 405 227 2011.
ISSN: ISSN 0022-2836
PubMed: 21040728
DOI: 10.1016/J.JMB.2010.10.048
Page generated: Wed Jul 31 01:24:56 2024

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