Atomistry » Copper » PDB 3mnd-3qjo » 3nq0
Atomistry »
  Copper »
    PDB 3mnd-3qjo »
      3nq0 »

Copper in PDB 3nq0: Crystal Structure of Tyrosinase From Bacillus Megaterium Crystallized in the Absence of Zinc

Enzymatic activity of Crystal Structure of Tyrosinase From Bacillus Megaterium Crystallized in the Absence of Zinc

All present enzymatic activity of Crystal Structure of Tyrosinase From Bacillus Megaterium Crystallized in the Absence of Zinc:
1.14.18.1;

Protein crystallography data

The structure of Crystal Structure of Tyrosinase From Bacillus Megaterium Crystallized in the Absence of Zinc, PDB code: 3nq0 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) 41.27 / 2.20
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 47.820, 78.700, 85.580, 90.00, 105.29, 90.00
R / Rfree (%) 24.2 / 29.2

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Tyrosinase From Bacillus Megaterium Crystallized in the Absence of Zinc (pdb code 3nq0). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Crystal Structure of Tyrosinase From Bacillus Megaterium Crystallized in the Absence of Zinc, PDB code: 3nq0:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 3nq0

Go back to Copper Binding Sites List in 3nq0
Copper binding site 1 out of 2 in the Crystal Structure of Tyrosinase From Bacillus Megaterium Crystallized in the Absence of Zinc


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 Crystallized in the Absence of Zinc within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:31.9
occ:1.00
NE2 A:HIS60 2.2 12.7 1.0
O A:HOH394 2.2 11.8 1.0
NE2 A:HIS69 2.2 10.6 1.0
NE2 A:HIS42 2.2 12.9 1.0
CD2 A:HIS60 3.1 6.9 1.0
CD2 A:HIS42 3.1 9.6 1.0
CD2 A:HIS69 3.2 10.0 1.0
CE1 A:HIS69 3.2 7.5 1.0
CE1 A:HIS60 3.3 15.6 1.0
CE1 A:HIS42 3.3 14.2 1.0
NE2 A:HIS231 3.8 9.8 1.0
CZ A:PHE227 3.9 6.7 1.0
CE2 A:PHE227 4.1 6.8 1.0
CE1 A:HIS231 4.1 8.7 1.0
CG A:HIS60 4.3 8.1 1.0
ND1 A:HIS69 4.3 6.4 1.0
CG A:HIS69 4.3 8.9 1.0
CG A:HIS42 4.3 9.3 1.0
ND1 A:HIS60 4.3 8.5 1.0
ND1 A:HIS42 4.4 11.1 1.0
CG1 A:VAL218 4.4 12.2 1.0
NE2 A:HIS204 4.7 11.2 1.0
CD2 A:HIS231 4.7 7.7 1.0
CE1 A:PHE65 4.8 6.0 1.0

Copper binding site 2 out of 2 in 3nq0

Go back to Copper Binding Sites List in 3nq0
Copper binding site 2 out of 2 in the Crystal Structure of Tyrosinase From Bacillus Megaterium Crystallized in the Absence of Zinc


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 Crystallized in the Absence of Zinc within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu502

b:34.6
occ:1.00
NE2 B:HIS69 2.2 6.6 1.0
NE2 B:HIS42 2.2 14.5 1.0
NE2 B:HIS60 2.2 15.6 1.0
O B:HOH304 2.3 18.6 1.0
CE1 B:HIS69 2.8 11.9 1.0
CE1 B:HIS42 3.0 16.9 1.0
CD2 B:HIS60 3.0 13.1 1.0
CE1 B:HIS60 3.3 17.9 1.0
CD2 B:HIS69 3.4 13.3 1.0
CD2 B:HIS42 3.4 12.3 1.0
NE2 B:HIS231 3.7 16.2 1.0
CZ B:PHE227 3.9 7.2 1.0
CE1 B:HIS231 3.9 14.6 1.0
ND1 B:HIS69 4.0 5.5 1.0
ND1 B:HIS42 4.2 13.5 1.0
CE2 B:PHE227 4.2 10.4 1.0
CG B:HIS60 4.3 19.6 1.0
CG B:HIS69 4.3 12.1 1.0
CG1 B:VAL218 4.3 22.9 1.0
ND1 B:HIS60 4.4 14.6 1.0
NE2 B:HIS204 4.4 18.6 1.0
CG B:HIS42 4.4 10.4 1.0
CE1 B:PHE65 4.7 9.7 1.0
CD2 B:HIS231 4.8 8.8 1.0
CE1 B:HIS204 4.8 18.1 1.0
ND1 B:HIS231 5.0 14.1 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: Sun Dec 13 11:11:00 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy