Cadmium in PDB 1fye: Aspartyl Dipeptidase (Anisotropic B-Factor Refinement)

The structure of Aspartyl Dipeptidase (Anisotropic B-Factor Refinement), PDB code: 1fye was solved by K.Hakansson, A.H.-J.Wang, C.G.Miller, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.20
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	91.986, 42.690, 62.496, 90.00, 106.06, 90.00
R / Rfree (%)	15.9 / 19.1

The binding sites of Cadmium atom in the Aspartyl Dipeptidase (Anisotropic B-Factor Refinement) (pdb code 1fye). This binding sites where shown within 5.0 Angstroms radius around Cadmium atom.
In total only one binding site of Cadmium was determined in the Aspartyl Dipeptidase (Anisotropic B-Factor Refinement), PDB code: 1fye:

Cadmium binding site 1 out of 1 in the Aspartyl Dipeptidase (Anisotropic B-Factor Refinement)


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 1 of Aspartyl Dipeptidase (Anisotropic B-Factor Refinement) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cd1001 b:16.6 occ:1.00 ND1 A:HIS227 2.3 14.0 1.0 OE2 A:GLU224 2.4 20.8 1.0 O A:HOH1068 2.4 24.5 1.0 O A:HOH1110 2.4 21.0 1.0 OE1 A:GLU224 2.5 23.0 1.0 CD A:GLU224 2.8 21.0 1.0 CE1 A:HIS227 3.1 17.1 1.0 CG A:HIS227 3.4 14.9 1.0 CB A:HIS227 3.8 13.4 1.0 O A:HOH1119 4.3 30.1 1.0 NE2 A:HIS227 4.3 19.0 1.0 CG A:GLU224 4.3 18.4 1.0 CA A:HIS227 4.4 14.9 1.0 CD2 A:HIS227 4.5 18.0 1.0 O A:HOH1053 4.5 19.0 1.0 O A:HOH1069 4.5 26.2 1.0 O A:HOH1173 4.8 30.0 1.0 N A:GLU224 4.8 20.3 1.0 CD2 A:LEU223 4.8 22.1 1.0

K.Hakansson, A.H.Wang, C.G.Miller. The Structure of Aspartyl Dipeptidase Reveals A Unique Fold with A Ser-His-Glu Catalytic Triad. Proc.Natl.Acad.Sci.Usa V. 97 14097 2000.
ISSN: ISSN 0027-8424
PubMed: 11106384
DOI: 10.1073/PNAS.260376797