Copper in PDB 2gi0: Crystal Structure of Cu(I) PHE114PRO Azurin Mutant

The structure of Crystal Structure of Cu(I) PHE114PRO Azurin Mutant, PDB code: 2gi0 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)	47.80 / 1.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	35.390, 47.860, 132.550, 90.00, 90.00, 90.00
R / Rfree (%)	17.9 / 22.4

The binding sites of Copper atom in the Crystal Structure of Cu(I) PHE114PRO Azurin Mutant (pdb code 2gi0). 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 Cu(I) PHE114PRO Azurin Mutant, PDB code: 2gi0:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Crystal Structure of Cu(I) PHE114PRO Azurin 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 Cu(I) PHE114PRO Azurin Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu200 b:17.6 occ:0.90 ND1 A:HIS117 2.0 12.1 1.0 ND1 A:HIS46 2.1 14.3 1.0 SG A:CYS112 2.3 14.3 1.0 SD A:MET121 2.8 16.0 1.0 CE1 A:HIS117 3.0 10.0 1.0 CE1 A:HIS46 3.0 13.2 1.0 CG A:HIS117 3.0 11.1 1.0 CG A:HIS46 3.2 11.8 1.0 CB A:CYS112 3.3 13.0 1.0 CB A:HIS117 3.4 13.0 1.0 CE A:MET121 3.4 16.5 1.0 CB A:HIS46 3.6 10.4 1.0 CA A:HIS46 3.7 11.1 1.0 O A:GLY45 3.8 9.9 1.0 NE2 A:HIS117 4.1 12.5 1.0 NE2 A:HIS46 4.1 17.4 1.0 CD2 A:HIS117 4.1 12.0 1.0 CD2 A:HIS46 4.2 11.2 1.0 CG A:PRO114 4.3 10.2 1.0 CD A:PRO114 4.3 12.9 1.0 CG A:MET121 4.3 15.0 1.0 CB A:MET121 4.6 14.3 1.0 N A:HIS46 4.6 10.6 1.0 C A:GLY45 4.6 11.5 1.0 CA A:CYS112 4.7 11.4 1.0 N A:ASN47 4.7 10.1 1.0 C A:HIS46 4.8 12.1 1.0 CA A:HIS117 4.8 13.2 1.0 CB A:PRO114 4.9 9.5 1.0 C A:CYS112 5.0 11.6 1.0

Copper binding site 2 out of 2 in the Crystal Structure of Cu(I) PHE114PRO Azurin 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 Cu(I) PHE114PRO Azurin Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu200 b:16.8 occ:0.90 ND1 B:HIS117 2.0 10.7 1.0 ND1 B:HIS46 2.1 13.6 1.0 SG B:CYS112 2.2 13.7 1.0 SD B:MET121 2.6 15.0 1.0 CE1 B:HIS117 3.0 10.9 1.0 CE1 B:HIS46 3.0 8.9 1.0 CG B:HIS117 3.1 11.4 1.0 CG B:HIS46 3.2 11.5 1.0 CB B:CYS112 3.3 13.2 1.0 CE B:MET121 3.4 21.2 1.0 CB B:HIS117 3.5 13.2 1.0 CB B:HIS46 3.6 9.7 1.0 CA B:HIS46 3.7 9.6 1.0 O B:GLY45 3.8 10.9 1.0 NE2 B:HIS117 4.1 10.8 1.0 NE2 B:HIS46 4.2 14.0 1.0 CD2 B:HIS117 4.2 13.1 1.0 CG B:MET121 4.2 16.5 1.0 CD B:PRO114 4.2 11.1 1.0 CG B:PRO114 4.2 11.1 1.0 CD2 B:HIS46 4.2 11.6 1.0 CB B:MET121 4.5 15.1 1.0 N B:HIS46 4.6 10.6 1.0 C B:GLY45 4.6 11.2 1.0 CA B:CYS112 4.7 11.9 1.0 N B:ASN47 4.7 8.6 1.0 C B:HIS46 4.8 10.0 1.0 CB B:PRO114 4.8 10.2 1.0 CA B:HIS117 4.8 13.8 1.0 CG B:MET13 4.9 23.7 1.0 C B:CYS112 4.9 12.6 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