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Copper in PDB 3sqr: Crystal Structure of Laccase From Botrytis Aclada at 1.67 A Resolution

Enzymatic activity of Crystal Structure of Laccase From Botrytis Aclada at 1.67 A Resolution

All present enzymatic activity of Crystal Structure of Laccase From Botrytis Aclada at 1.67 A Resolution:
1.10.3.2;

Protein crystallography data

The structure of Crystal Structure of Laccase From Botrytis Aclada at 1.67 A Resolution, PDB code: 3sqr 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) 75.67 / 1.67
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 69.670, 113.500, 79.910, 90.00, 108.75, 90.00
R / Rfree (%) 16.5 / 19.1

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Laccase From Botrytis Aclada at 1.67 A Resolution (pdb code 3sqr). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the Crystal Structure of Laccase From Botrytis Aclada at 1.67 A Resolution, PDB code: 3sqr:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in 3sqr

Go back to Copper Binding Sites List in 3sqr
Copper binding site 1 out of 3 in the Crystal Structure of Laccase From Botrytis Aclada at 1.67 A Resolution


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 Laccase From Botrytis Aclada at 1.67 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu544

b:25.4
occ:1.00
ND1 A:HIS426 2.0 22.1 1.0
ND1 A:HIS494 2.0 23.2 1.0
SG A:CYS489 2.2 23.4 1.0
CG A:HIS494 2.9 24.1 1.0
CE1 A:HIS426 3.0 26.0 1.0
CG A:HIS426 3.0 26.7 1.0
CE1 A:HIS494 3.1 24.5 1.0
CB A:CYS489 3.2 23.0 1.0
CB A:HIS494 3.2 24.6 1.0
CB A:HIS426 3.4 25.2 1.0
CD1 A:ILE491 3.5 22.7 1.0
CD1 A:LEU499 3.6 24.9 1.0
CA A:HIS426 4.0 25.0 1.0
CB A:ILE491 4.1 19.3 1.0
NE2 A:HIS426 4.1 24.4 1.0
CD2 A:HIS494 4.1 23.5 1.0
NE2 A:HIS494 4.1 23.6 1.0
CG1 A:ILE491 4.1 22.4 1.0
CD2 A:HIS426 4.2 26.6 1.0
CA A:CYS489 4.6 21.1 1.0
CD A:PRO427 4.7 22.1 1.0
CA A:HIS494 4.8 24.2 1.0
CG2 A:ILE424 4.9 25.1 1.0
CG A:LEU499 4.9 21.6 1.0
CG2 A:ILE491 4.9 22.3 1.0
C A:HIS426 5.0 23.4 1.0
N A:ILE491 5.0 22.6 1.0

Copper binding site 2 out of 3 in 3sqr

Go back to Copper Binding Sites List in 3sqr
Copper binding site 2 out of 3 in the Crystal Structure of Laccase From Botrytis Aclada at 1.67 A Resolution


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 Laccase From Botrytis Aclada at 1.67 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu545

b:27.4
occ:0.80
NE2 A:HIS488 2.0 25.6 1.0
NE2 A:HIS431 2.0 21.4 1.0
NE2 A:HIS133 2.1 23.0 1.0
O A:HOH811 2.1 31.2 1.0
ND1 A:HIS429 2.8 29.2 1.0
CE1 A:HIS431 2.9 20.7 1.0
CD2 A:HIS488 2.9 26.1 1.0
CE1 A:HIS488 3.0 24.3 1.0
CD2 A:HIS133 3.0 23.2 1.0
CD2 A:HIS431 3.1 19.6 1.0
CE1 A:HIS133 3.1 25.1 1.0
CE1 A:HIS429 3.3 26.4 1.0
CG A:HIS429 4.0 26.2 1.0
ND1 A:HIS431 4.0 20.1 1.0
CG A:HIS488 4.1 22.8 1.0
ND1 A:HIS488 4.1 24.4 1.0
O A:HOH618 4.1 34.7 1.0
CG A:HIS431 4.1 19.2 1.0
ND1 A:HIS133 4.2 22.3 1.0
CG A:HIS133 4.2 21.8 1.0
CD2 A:LEU486 4.2 22.9 1.0
CD2 A:HIS87 4.3 22.4 1.0
NE2 A:HIS87 4.4 24.0 1.0
NE2 A:HIS429 4.6 30.4 1.0
CB A:HIS429 4.6 25.1 1.0
CU A:CU546 4.6 27.4 0.8
NE2 A:HIS490 4.8 24.0 1.0
CD2 A:HIS490 4.8 23.3 1.0
CD2 A:HIS429 4.9 28.9 1.0
CG A:LEU486 5.0 22.4 1.0

Copper binding site 3 out of 3 in 3sqr

Go back to Copper Binding Sites List in 3sqr
Copper binding site 3 out of 3 in the Crystal Structure of Laccase From Botrytis Aclada at 1.67 A Resolution


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 Laccase From Botrytis Aclada at 1.67 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu546

b:27.4
occ:0.80
ND1 A:HIS89 2.0 21.7 1.0
NE2 A:HIS131 2.0 22.6 1.0
NE2 A:HIS490 2.1 24.0 1.0
O A:HOH811 2.6 31.2 1.0
CE1 A:HIS89 2.8 19.4 1.0
CE1 A:HIS131 2.9 24.7 1.0
CE1 A:HIS490 3.0 25.1 1.0
CD2 A:HIS131 3.1 22.1 1.0
CG A:HIS89 3.1 17.9 1.0
CD2 A:HIS490 3.2 23.3 1.0
CZ2 A:TRP129 3.5 22.5 1.0
CB A:HIS89 3.6 19.7 1.0
CE2 A:TRP129 3.9 22.7 1.0
NE2 A:HIS89 4.0 22.2 1.0
ND1 A:HIS429 4.0 29.2 1.0
CD2 A:HIS87 4.0 22.4 1.0
ND1 A:HIS131 4.0 21.3 1.0
CE1 A:HIS429 4.1 26.4 1.0
NE1 A:TRP129 4.1 23.7 1.0
CD2 A:HIS89 4.1 20.6 1.0
CG A:HIS131 4.2 19.5 1.0
ND1 A:HIS490 4.2 21.5 1.0
CH2 A:TRP129 4.2 20.8 1.0
CG A:HIS490 4.3 23.1 1.0
NE2 A:HIS87 4.5 24.0 1.0
O A:HOH618 4.6 34.7 1.0
CU A:CU545 4.6 27.4 0.8
CA A:HIS89 4.7 19.1 1.0
CG A:HIS429 4.8 26.2 1.0
NE2 A:HIS429 4.9 30.4 1.0
CD2 A:TRP129 4.9 22.0 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: Fri Sep 4 08:30:29 2020
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