Copper in PDB 1f1d: Crystal Structure of Yeast H46C Cuznsod Mutant

All present enzymatic activity of Crystal Structure of Yeast H46C Cuznsod Mutant:
1.15.1.1;

The structure of Crystal Structure of Yeast H46C Cuznsod Mutant, PDB code: 1f1d was solved by P.J.Hart, N.L.Ogihara, H.Liu, A.M.Nersissian, J.S.Valentine, D.Eisenberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	6.00 / 2.10
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	119.400, 119.400, 74.900, 90.00, 90.00, 120.00
R / Rfree (%)	23.3 / 27.8

The structure of Crystal Structure of Yeast H46C Cuznsod Mutant also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Copper atom in the Crystal Structure of Yeast H46C Cuznsod Mutant (pdb code 1f1d). 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 Crystal Structure of Yeast H46C Cuznsod Mutant, PDB code: 1f1d:

Copper binding site 1 out of 1 in the Crystal Structure of Yeast H46C Cuznsod 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 Yeast H46C Cuznsod Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu154 b:32.2 occ:1.00 NE2 A:HIS120 2.0 12.9 1.0 NE2 A:HIS48 2.2 13.5 1.0 SG A:CYS46 2.8 20.0 1.0 CD2 A:HIS120 2.9 12.0 1.0 CE1 A:HIS48 3.0 12.9 1.0 CE1 A:HIS120 3.0 12.3 1.0 NE2 A:HIS63 3.2 20.4 1.0 CD2 A:HIS48 3.3 13.6 1.0 CD2 A:HIS63 3.7 18.5 1.0 CB A:CYS46 4.0 15.2 1.0 CG1 A:VAL118 4.1 11.1 1.0 CG A:HIS120 4.1 13.2 1.0 ND1 A:HIS120 4.1 13.0 1.0 ND1 A:HIS48 4.2 14.0 1.0 CE1 A:HIS63 4.3 18.5 1.0 CB A:VAL118 4.4 11.1 1.0 CG A:HIS48 4.4 13.3 1.0 CA A:CYS46 4.9 13.8 1.0 CG A:HIS63 4.9 16.8 1.0 NE A:ARG143 4.9 12.9 1.0

P.J.Hart, M.M.Balbirnie, N.L.Ogihara, A.M.Nersissian, M.S.Weiss, J.S.Valentine, D.Eisenberg. A Structure-Based Mechanism For Copper-Zinc Superoxide Dismutase. Biochemistry V. 38 2167 1999.
ISSN: ISSN 0006-2960
PubMed: 10026301
DOI: 10.1021/BI982284U