Copper in PDB 3aav: Bovine Beta-Trypsin Bound to Meta-Diamidino Schiff Base Copper (II) Chelate

All present enzymatic activity of Bovine Beta-Trypsin Bound to Meta-Diamidino Schiff Base Copper (II) Chelate:
3.4.21.4;

The structure of Bovine Beta-Trypsin Bound to Meta-Diamidino Schiff Base Copper (II) Chelate, PDB code: 3aav was solved by D.Iyaguchi, S.Kawano, E.Toyota, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.70
Space group	P 31
Cell size a, b, c (Å), α, β, γ (°)	54.568, 54.568, 107.235, 90.00, 90.00, 120.00
R / Rfree (%)	18.3 / 20.9

The structure of Bovine Beta-Trypsin Bound to Meta-Diamidino Schiff Base Copper (II) Chelate also contains other interesting chemical elements:

Calcium

(Ca)

2 atoms

The binding sites of Copper atom in the Bovine Beta-Trypsin Bound to Meta-Diamidino Schiff Base Copper (II) Chelate (pdb code 3aav). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Bovine Beta-Trypsin Bound to Meta-Diamidino Schiff Base Copper (II) Chelate, PDB code: 3aav:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Bovine Beta-Trypsin Bound to Meta-Diamidino Schiff Base Copper (II) Chelate


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Bovine Beta-Trypsin Bound to Meta-Diamidino Schiff Base Copper (II) Chelate within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu3001 b:0.4 occ:1.00 O A:HOH400 1.2 60.9 1.0 OAP A:A2C1001 1.4 54.8 1.0 OAO A:A2C1001 2.2 55.6 1.0 O A:HOH402 2.4 48.4 1.0 OG A:SER177 2.5 20.4 1.0 NAV A:A2C1001 2.6 55.1 1.0 CAQ A:A2C1001 2.7 54.7 1.0 CAX A:A2C1001 3.0 55.9 1.0 CAW A:A2C1001 3.1 55.9 1.0 NAY A:A2C1001 3.2 56.0 1.0 O A:HOH386 3.3 27.6 1.0 CAF A:A2C1001 3.4 54.1 1.0 CAN A:A2C1001 3.4 57.2 1.0 CAU A:A2C1001 3.6 55.9 1.0 CAR A:A2C1001 3.7 54.5 1.0 CB A:SER177 3.9 15.5 1.0 CAM A:A2C1001 4.0 57.1 1.0 CAZ A:A2C1001 4.1 55.6 1.0 CA A:GLN174 4.1 20.5 1.0 NE2 A:HIS40 4.2 15.9 1.0 CAE A:A2C1001 4.4 57.9 1.0 N A:GLY175 4.6 15.9 1.0 CAG A:A2C1001 4.6 54.1 1.0 CG A:GLN174 4.6 31.0 1.0 O A:HOH274 4.7 31.6 1.0 N A:GLN174 4.8 19.7 1.0 CB A:GLN174 4.8 24.7 1.0 CAS A:A2C1001 4.8 54.3 1.0 O A:SER192 4.8 14.4 1.0 CA A:SER177 4.9 14.0 1.0 N A:SER177 4.9 13.8 1.0 O A:CYS173 4.9 17.4 1.0 C A:GLN174 5.0 18.8 1.0

Copper binding site 2 out of 2 in the Bovine Beta-Trypsin Bound to Meta-Diamidino Schiff Base Copper (II) Chelate


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Bovine Beta-Trypsin Bound to Meta-Diamidino Schiff Base Copper (II) Chelate within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu3002 b:0.9 occ:1.00 O B:HOH401 1.5 57.7 1.0 OAP B:A2C1002 1.5 55.4 1.0 OAO B:A2C1002 2.1 56.2 1.0 NAV B:A2C1002 2.2 55.8 1.0 OG B:SER177 2.2 20.6 1.0 CAW B:A2C1002 2.6 56.6 1.0 CAX B:A2C1002 2.6 56.6 1.0 CAQ B:A2C1002 2.9 55.2 1.0 NAY B:A2C1002 3.0 56.5 1.0 CAU B:A2C1002 3.2 56.4 1.0 CAN B:A2C1002 3.2 57.5 1.0 CB B:SER177 3.5 15.8 1.0 O B:HOH410 3.6 25.9 1.0 CAF B:A2C1002 3.7 55.0 1.0 CAM B:A2C1002 3.7 57.5 1.0 CAR B:A2C1002 3.7 55.3 1.0 CA B:GLN174 4.0 21.6 1.0 CAZ B:A2C1002 4.0 56.0 1.0 NE2 B:HIS40 4.2 16.9 1.0 N B:GLY175 4.2 17.4 1.0 CAE B:A2C1002 4.4 58.0 1.0 CA B:SER177 4.5 14.3 1.0 N B:SER177 4.5 13.9 1.0 CG B:GLN174 4.6 31.8 1.0 O B:CYS173 4.6 17.8 1.0 N B:GLN174 4.7 20.8 1.0 C B:GLN174 4.7 19.3 1.0 CB B:GLN174 4.7 25.1 1.0 CAS B:A2C1002 4.8 55.3 1.0 CAG B:A2C1002 4.9 55.1 1.0 C B:CYS173 4.9 20.1 1.0 O B:SER192 4.9 13.7 1.0 CE1 B:HIS40 5.0 16.9 1.0

D.Iyaguchi, S.Kawano, K.Takada, E.Toyota. Structural Basis For the Design of Novel Schiff Base Metal Chelate Inhibitors of Trypsin Bioorg.Med.Chem. V. 18 2076 2010.
ISSN: ISSN 0968-0896
PubMed: 20202854
DOI: 10.1016/J.BMC.2010.02.016