Copper in PDB 3sqr: 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;

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

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 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 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 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

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