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Copper in PDB 3v9e: Structure of the L499M Mutant of the Laccase From B.Aclada

Enzymatic activity of Structure of the L499M Mutant of the Laccase From B.Aclada

All present enzymatic activity of Structure of the L499M Mutant of the Laccase From B.Aclada:
1.10.3.2;

Protein crystallography data

The structure of Structure of the L499M Mutant of the Laccase From B.Aclada, PDB code: 3v9e was solved by E.M.Osipov, K.M.Polyakov, T.V.Tikhonova, P.V.Dorovatovsky, R.Ludwig, R.Kittl, S.V.Shleev, V.O.Popov, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.55 / 1.70
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 69.710, 113.560, 79.980, 90.00, 108.74, 90.00
R / Rfree (%) 16.3 / 20

Copper Binding Sites:

The binding sites of Copper atom in the Structure of the L499M Mutant of the Laccase From B.Aclada (pdb code 3v9e). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the Structure of the L499M Mutant of the Laccase From B.Aclada, PDB code: 3v9e:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in 3v9e

Go back to Copper Binding Sites List in 3v9e
Copper binding site 1 out of 3 in the Structure of the L499M Mutant of the Laccase From B.Aclada


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Structure of the L499M Mutant of the Laccase From B.Aclada within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu601

b:19.2
occ:1.00
ND1 A:HIS426 2.0 15.6 1.0
ND1 A:HIS494 2.0 16.7 1.0
SG A:CYS489 2.2 16.5 1.0
CE1 A:HIS426 3.0 18.1 1.0
CG A:HIS494 3.0 15.9 1.0
CE1 A:HIS494 3.0 19.2 1.0
CG A:HIS426 3.0 17.1 1.0
SD A:MET499 3.2 17.6 1.0
CB A:CYS489 3.2 15.8 1.0
CB A:HIS494 3.3 14.7 1.0
CB A:HIS426 3.4 17.8 1.0
CD1 A:ILE491 3.7 15.3 1.0
CE A:MET499 3.8 17.9 1.0
NE2 A:HIS426 4.1 18.5 1.0
NE2 A:HIS494 4.1 18.8 1.0
CA A:HIS426 4.1 17.1 1.0
CD2 A:HIS494 4.1 17.6 1.0
CD2 A:HIS426 4.1 18.1 1.0
CB A:ILE491 4.2 13.4 1.0
CG1 A:ILE491 4.3 14.5 1.0
CA A:CYS489 4.6 14.8 1.0
CG A:MET499 4.6 16.2 1.0
CA A:HIS494 4.8 16.2 1.0
CD A:PRO427 4.9 14.9 1.0
CB A:MET499 4.9 17.0 1.0
CG2 A:ILE424 5.0 19.3 1.0

Copper binding site 2 out of 3 in 3v9e

Go back to Copper Binding Sites List in 3v9e
Copper binding site 2 out of 3 in the Structure of the L499M Mutant of the Laccase From B.Aclada


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Structure of the L499M Mutant of the Laccase From B.Aclada within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu602

b:20.0
occ:0.80
NE2 A:HIS431 2.0 14.2 1.0
NE2 A:HIS488 2.0 17.2 1.0
O A:HOH867 2.0 18.1 1.0
NE2 A:HIS133 2.2 17.6 1.0
ND1 A:HIS429 2.6 20.9 1.0
CE1 A:HIS431 2.8 13.7 1.0
CE1 A:HIS488 2.9 17.7 1.0
CD2 A:HIS488 3.0 16.3 1.0
CD2 A:HIS431 3.1 14.6 1.0
CD2 A:HIS133 3.1 16.3 1.0
CE1 A:HIS133 3.2 18.6 1.0
CE1 A:HIS429 3.2 20.2 1.0
CG A:HIS429 3.8 18.9 1.0
ND1 A:HIS431 4.0 13.1 1.0
ND1 A:HIS488 4.1 16.8 1.0
CG A:HIS488 4.1 15.5 1.0
CG A:HIS431 4.1 12.1 1.0
O A:HOH716 4.1 21.6 1.0
ND1 A:HIS133 4.3 15.3 1.0
CG A:HIS133 4.3 16.3 1.0
CD2 A:HIS87 4.4 14.3 1.0
CD2 A:LEU486 4.4 16.1 1.0
NE2 A:HIS87 4.4 15.1 1.0
CB A:HIS429 4.4 18.8 1.0
NE2 A:HIS429 4.4 20.0 1.0
CU A:CU603 4.7 24.0 0.8
CD2 A:HIS429 4.7 18.5 1.0
CD2 A:HIS490 4.9 20.6 1.0
NE2 A:HIS490 4.9 19.2 1.0

Copper binding site 3 out of 3 in 3v9e

Go back to Copper Binding Sites List in 3v9e
Copper binding site 3 out of 3 in the Structure of the L499M Mutant of the Laccase From B.Aclada


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Structure of the L499M Mutant of the Laccase From B.Aclada within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu603

b:24.0
occ:0.80
ND1 A:HIS89 1.8 16.8 1.0
NE2 A:HIS131 2.0 14.6 1.0
NE2 A:HIS490 2.3 19.2 1.0
CE1 A:HIS89 2.6 15.7 1.0
CE1 A:HIS131 2.9 16.3 1.0
O A:HOH867 2.9 18.1 1.0
CG A:HIS89 3.0 13.6 1.0
CD2 A:HIS131 3.1 15.8 1.0
CE1 A:HIS490 3.2 20.4 1.0
CZ2 A:TRP129 3.3 15.0 1.0
CD2 A:HIS490 3.4 20.6 1.0
CB A:HIS89 3.6 13.8 1.0
CE2 A:TRP129 3.7 14.5 1.0
NE2 A:HIS89 3.8 16.1 1.0
NE1 A:TRP129 3.8 14.7 1.0
CD2 A:HIS89 4.0 15.6 1.0
ND1 A:HIS131 4.0 16.2 1.0
CH2 A:TRP129 4.1 13.7 1.0
CD2 A:HIS87 4.1 14.3 1.0
ND1 A:HIS429 4.2 20.9 1.0
CG A:HIS131 4.2 13.9 1.0
CE1 A:HIS429 4.2 20.2 1.0
ND1 A:HIS490 4.4 20.2 1.0
CG A:HIS490 4.5 17.8 1.0
CA A:HIS89 4.6 13.8 1.0
NE2 A:HIS87 4.6 15.1 1.0
O A:HOH716 4.6 21.6 1.0
CD2 A:TRP129 4.7 12.7 1.0
CU A:CU602 4.7 20.0 0.8
CD1 A:TRP129 4.9 14.6 1.0
NE2 A:HIS429 4.9 20.0 1.0
CG A:HIS429 4.9 18.9 1.0

Reference:

E.Osipov, K.Polyakov, R.Kittl, S.Shleev, P.Dorovatovsky, T.Tikhonova, S.Hann, R.Ludwig, V.Popov. Effect of the L499M Mutation of the Ascomycetous Botrytis Aclada Laccase on Redox Potential and Catalytic Properties. Acta Crystallogr.,Sect.D V. 70 2913 2014.
ISSN: ISSN 0907-4449
PubMed: 25372682
DOI: 10.1107/S1399004714020380
Page generated: Sun Dec 13 11:12:36 2020

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