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Copper in PDB 4nb7: Crystal Structure of Two-Domain Laccase From Streptomyces Lividans AC1709 in Complex with Azide After 180 Min Soaking

Enzymatic activity of Crystal Structure of Two-Domain Laccase From Streptomyces Lividans AC1709 in Complex with Azide After 180 Min Soaking

All present enzymatic activity of Crystal Structure of Two-Domain Laccase From Streptomyces Lividans AC1709 in Complex with Azide After 180 Min Soaking:
1.10.3.2;

Protein crystallography data

The structure of Crystal Structure of Two-Domain Laccase From Streptomyces Lividans AC1709 in Complex with Azide After 180 Min Soaking, PDB code: 4nb7 was solved by A.Gabdulkhakov, S.Tischenko, L.Yurevich, A.Lisov, A.Leontievsky, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.38 / 2.55
Space group P 43 3 2
Cell size a, b, c (Å), α, β, γ (°) 177.510, 177.510, 177.510, 90.00, 90.00, 90.00
R / Rfree (%) 16.1 / 18.1

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Two-Domain Laccase From Streptomyces Lividans AC1709 in Complex with Azide After 180 Min Soaking (pdb code 4nb7). 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 Two-Domain Laccase From Streptomyces Lividans AC1709 in Complex with Azide After 180 Min Soaking, PDB code: 4nb7:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 4nb7

Go back to Copper Binding Sites List in 4nb7
Copper binding site 1 out of 4 in the Crystal Structure of Two-Domain Laccase From Streptomyces Lividans AC1709 in Complex with Azide After 180 Min Soaking


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 Two-Domain Laccase From Streptomyces Lividans AC1709 in Complex with Azide After 180 Min Soaking within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu401

b:52.1
occ:1.00
ND1 A:HIS293 1.9 47.4 1.0
ND1 A:HIS231 2.1 53.4 1.0
SG A:CYS288 2.1 50.4 1.0
CE1 A:HIS293 2.9 49.1 1.0
CG A:HIS231 2.9 49.6 1.0
CG A:HIS293 3.0 49.3 1.0
CE1 A:HIS231 3.1 49.3 1.0
CB A:HIS231 3.1 46.3 1.0
CB A:CYS288 3.2 46.0 1.0
CB A:HIS293 3.4 48.2 1.0
SD A:MET298 3.6 53.8 1.0
CA A:HIS231 3.6 47.4 1.0
CE A:MET298 3.9 49.1 1.0
CG2 A:VAL290 4.0 46.4 1.0
NE2 A:HIS293 4.0 49.5 1.0
O A:TYR230 4.1 46.8 1.0
CD2 A:HIS293 4.1 44.5 1.0
CB A:VAL290 4.1 46.1 1.0
CD2 A:HIS231 4.1 49.5 1.0
NE2 A:HIS231 4.2 49.5 1.0
CA A:CYS288 4.6 47.1 1.0
N A:THR232 4.6 46.3 1.0
N A:HIS231 4.6 49.7 1.0
C A:HIS231 4.7 48.5 1.0
C A:TYR230 4.8 48.3 1.0
CD2 A:PHE195 4.8 48.7 1.0
CA A:HIS293 4.9 49.4 1.0
CG1 A:VAL290 5.0 45.0 1.0

Copper binding site 2 out of 4 in 4nb7

Go back to Copper Binding Sites List in 4nb7
Copper binding site 2 out of 4 in the Crystal Structure of Two-Domain Laccase From Streptomyces Lividans AC1709 in Complex with Azide After 180 Min Soaking


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 Two-Domain Laccase From Streptomyces Lividans AC1709 in Complex with Azide After 180 Min Soaking within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu402

b:51.1
occ:1.00
NE2 A:HIS289 2.1 45.3 1.0
O A:HOH531 2.6 60.3 1.0
CD2 A:HIS289 3.0 45.5 1.0
CE1 A:HIS289 3.0 48.4 1.0
ND1 A:HIS289 4.1 46.8 1.0
CG A:HIS289 4.1 45.9 1.0
NE2 A:HIS234 4.2 52.5 1.0
CU A:CU404 4.2 54.4 0.3
CD2 A:HIS234 4.3 51.6 1.0
O A:HOH532 4.7 56.6 1.0
CE1 A:HIS234 4.9 49.0 1.0

Copper binding site 3 out of 4 in 4nb7

Go back to Copper Binding Sites List in 4nb7
Copper binding site 3 out of 4 in the Crystal Structure of Two-Domain Laccase From Streptomyces Lividans AC1709 in Complex with Azide After 180 Min Soaking


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 Two-Domain Laccase From Streptomyces Lividans AC1709 in Complex with Azide After 180 Min Soaking within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu403

b:61.1
occ:1.00
NE2 A:HIS236 2.1 51.4 1.0
NE2 A:HIS287 2.3 50.1 1.0
O A:HOH531 2.7 60.3 1.0
CE1 A:HIS236 2.9 51.1 1.0
CE1 A:HIS287 3.2 48.5 1.0
CD2 A:HIS287 3.2 52.3 1.0
CD2 A:HIS236 3.2 49.6 1.0
O A:HOH532 3.6 56.6 1.0
CD2 A:HIS234 4.1 51.6 1.0
ND1 A:HIS236 4.1 54.5 1.0
ND1 A:HIS287 4.2 53.2 1.0
CG A:HIS236 4.3 50.8 1.0
CE A:MET285 4.3 58.2 1.0
CG A:HIS287 4.3 50.9 1.0
CU A:CU404 4.4 54.4 0.3
NE2 A:HIS234 4.5 52.5 1.0
SD A:MET285 4.6 67.6 0.8
NE2 A:HIS289 5.0 45.3 1.0

Copper binding site 4 out of 4 in 4nb7

Go back to Copper Binding Sites List in 4nb7
Copper binding site 4 out of 4 in the Crystal Structure of Two-Domain Laccase From Streptomyces Lividans AC1709 in Complex with Azide After 180 Min Soaking


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 Two-Domain Laccase From Streptomyces Lividans AC1709 in Complex with Azide After 180 Min Soaking within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu404

b:54.4
occ:0.33
NE2 A:HIS234 2.0 52.5 1.0
CE1 A:HIS234 2.8 49.0 1.0
O A:HOH531 3.0 60.3 1.0
CD2 A:HIS234 3.2 51.6 1.0
CD2 A:HIS236 3.4 49.6 1.0
NE2 A:HIS236 3.6 51.4 1.0
CG A:HIS236 3.9 50.8 1.0
ND1 A:HIS234 4.0 48.8 1.0
CE1 A:HIS236 4.1 51.1 1.0
CG A:HIS234 4.2 52.2 1.0
CU A:CU402 4.2 51.1 1.0
ND1 A:HIS236 4.3 54.5 1.0
CU A:CU403 4.4 61.1 1.0
CA A:HIS236 4.4 48.5 1.0
CB A:HIS236 4.7 51.1 1.0
O A:MET235 4.8 48.1 1.0
N A:HIS236 4.8 50.2 1.0
OD2 A:ASP259 4.9 54.7 1.0
C A:MET235 5.0 48.6 1.0

Reference:

A.Gabdulkhakov, S.Tischenko, L.Yurevich, A.Lisov, A.Leontievsky. Crystal Structure of Two-Domain Laccase From Streptomyces Lividans AC1709 in Complex with Azide After 180 Min Soaking To Be Published.
Page generated: Sun Dec 13 11:15:22 2020

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