Copper in PDB 2ghz: Crystal Structure of Azurin PHE114PRO Mutant

The structure of Crystal Structure of Azurin PHE114PRO Mutant, PDB code: 2ghz was solved by S.Yanagisawa, M.J.Banfield, C.Dennison, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.80 / 1.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	35.350, 47.810, 132.520, 90.00, 90.00, 90.00
R / Rfree (%)	14.2 / 19

The binding sites of Copper atom in the Crystal Structure of Azurin PHE114PRO Mutant (pdb code 2ghz). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Crystal Structure of Azurin PHE114PRO Mutant, PDB code: 2ghz:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Crystal Structure of Azurin PHE114PRO Mutant


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 Azurin PHE114PRO Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu200 b:15.6 occ:0.90 ND1 A:HIS117 2.0 14.8 1.0 ND1 A:HIS46 2.1 14.6 1.0 SG A:CYS112 2.2 14.2 1.0 CE1 A:HIS46 2.9 13.4 1.0 CE1 A:HIS117 2.9 13.9 1.0 SD A:MET121 3.0 16.4 1.0 CG A:HIS117 3.0 14.1 1.0 CG A:HIS46 3.1 12.2 1.0 CB A:CYS112 3.2 13.9 1.0 CB A:HIS117 3.4 13.5 1.0 CB A:HIS46 3.5 12.9 1.0 CA A:HIS46 3.6 12.2 1.0 O A:GLY45 3.6 12.4 1.0 CE A:MET121 3.6 17.0 1.0 NE2 A:HIS117 4.1 15.8 1.0 CG A:PRO114 4.1 11.4 1.0 NE2 A:HIS46 4.1 14.8 1.0 CD2 A:HIS117 4.1 15.2 1.0 CD2 A:HIS46 4.2 14.1 1.0 CD A:PRO114 4.2 12.1 1.0 C A:GLY45 4.4 12.8 1.0 N A:HIS46 4.4 11.6 1.0 CG A:MET121 4.5 15.4 1.0 CA A:CYS112 4.6 12.0 1.0 CB A:PRO114 4.6 11.4 1.0 N A:ASN47 4.6 10.7 1.0 C A:HIS46 4.7 11.5 1.0 CB A:MET121 4.8 15.4 1.0 CA A:HIS117 4.8 15.6 1.0 C A:CYS112 4.8 12.5 1.0

Copper binding site 2 out of 2 in the Crystal Structure of Azurin PHE114PRO Mutant


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 Azurin PHE114PRO Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu200 b:14.8 occ:0.90 ND1 B:HIS117 2.0 13.9 1.0 ND1 B:HIS46 2.1 14.4 1.0 SG B:CYS112 2.1 13.8 1.0 SD B:MET121 2.8 14.0 1.0 CE1 B:HIS117 2.9 13.8 1.0 CE1 B:HIS46 3.0 11.2 1.0 CG B:HIS117 3.0 13.2 1.0 CG B:HIS46 3.1 12.1 1.0 CB B:CYS112 3.3 14.1 1.0 CB B:HIS117 3.4 13.5 1.0 CE B:MET121 3.5 17.6 1.0 CB B:HIS46 3.5 12.2 1.0 CA B:HIS46 3.6 11.2 1.0 O B:GLY45 3.6 12.7 1.0 NE2 B:HIS117 4.1 13.8 1.0 CD2 B:HIS117 4.1 15.6 1.0 CG B:PRO114 4.1 13.4 1.0 NE2 B:HIS46 4.1 13.0 1.0 CD B:PRO114 4.2 13.4 1.0 CD2 B:HIS46 4.2 14.1 1.0 CG B:MET121 4.4 15.4 1.0 C B:GLY45 4.4 11.8 1.0 N B:HIS46 4.4 11.2 1.0 CA B:CYS112 4.5 11.5 1.0 N B:ASN47 4.6 10.2 1.0 CB B:PRO114 4.6 13.4 1.0 C B:HIS46 4.7 10.7 1.0 CB B:MET121 4.7 15.0 1.0 C B:CYS112 4.8 12.4 1.0 CA B:HIS117 4.8 14.8 1.0 O B:CYS112 5.0 14.1 1.0

S.Yanagisawa, M.J.Banfield, C.Dennison. The Role of Hydrogen Bonding at the Active Site of A Cupredoxin: the PHE114PRO Azurin Variant. Biochemistry V. 45 8812 2006.
ISSN: ISSN 0006-2960
PubMed: 16846224
DOI: 10.1021/BI0606851