Copper in PDB 1sf5: Structure of Oxidized State of the P94A Mutant of Amicyanin

The structure of Structure of Oxidized State of the P94A Mutant of Amicyanin, PDB code: 1sf5 was solved by C.J.Carrell, D.Sun, S.Jiang, V.L.Davidson, F.S.Mathews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	28.396, 55.434, 27.095, 90.00, 95.17, 90.00
R / Rfree (%)	12.7 / 16.6

The binding sites of Copper atom in the Structure of Oxidized State of the P94A Mutant of Amicyanin (pdb code 1sf5). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Structure of Oxidized State of the P94A Mutant of Amicyanin, PDB code: 1sf5:

Copper binding site 1 out of 1 in the Structure of Oxidized State of the P94A Mutant of Amicyanin


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Structure of Oxidized State of the P94A Mutant of Amicyanin within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu107 b:18.8 occ:1.00 SG A:CYS92 2.0 12.7 1.0 ND1 A:HIS53 2.1 13.0 1.0 ND1 A:HIS95 2.1 15.3 1.0 CE1 A:HIS53 3.0 14.6 1.0 CE1 A:HIS95 3.0 17.8 1.0 CG A:HIS53 3.1 10.9 1.0 CG A:HIS95 3.1 13.6 1.0 SD A:MET98 3.1 15.0 1.0 CB A:CYS92 3.2 9.1 1.0 CB A:HIS95 3.5 14.9 1.0 CB A:HIS53 3.5 10.4 1.0 CA A:HIS53 3.7 9.9 1.0 O A:PRO52 3.8 13.8 1.0 CE A:MET98 4.0 21.4 1.0 NE2 A:HIS53 4.1 13.7 1.0 N A:HIS95 4.2 12.1 1.0 NE2 A:HIS95 4.2 16.9 1.0 CD2 A:HIS53 4.2 13.3 1.0 CD2 A:HIS95 4.2 15.7 1.0 CA A:HIS95 4.4 12.5 1.0 CA A:CYS92 4.5 8.5 1.0 C A:PRO52 4.6 11.9 1.0 N A:ASN54 4.6 9.0 1.0 N A:HIS53 4.6 10.5 1.0 CG A:MET98 4.6 12.6 1.0 CB A:ALA94 4.7 20.1 1.0 C A:HIS53 4.7 9.7 1.0 O A:HIS95 4.8 11.7 1.0 CE A:MET28 4.9 29.7 0.6

C.J.Carrell, D.Sun, S.Jiang, V.L.Davidson, F.S.Mathews. Structural Studies of Two Mutants of Amicyanin From Paracoccus Denitrificans That Stabilize the Reduced State of the Copper. Biochemistry V. 43 9372 2004.
ISSN: ISSN 0006-2960
PubMed: 15260480
DOI: 10.1021/BI049634Z