Zinc in PDB 3cww: Crystal Structure of Ide-Bradykinin Complex

All present enzymatic activity of Crystal Structure of Ide-Bradykinin Complex:
3.4.24.56;

The structure of Crystal Structure of Ide-Bradykinin Complex, PDB code: 3cww was solved by E.Malito, W.J.Tang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.77 / 1.96
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	262.448, 262.448, 90.628, 90.00, 90.00, 120.00
R / Rfree (%)	18.1 / 20.8

The binding sites of Zinc atom in the Crystal Structure of Ide-Bradykinin Complex (pdb code 3cww). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Ide-Bradykinin Complex, PDB code: 3cww:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Ide-Bradykinin Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Ide-Bradykinin Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn2002 b:23.7 occ:1.00 OE1 A:GLU189 1.9 18.8 1.0 NE2 A:HIS112 2.0 21.0 1.0 NE2 A:HIS108 2.1 19.2 1.0 CD A:GLU189 2.7 24.9 1.0 OE2 A:GLU189 2.8 26.1 1.0 CE1 A:HIS108 3.0 19.5 1.0 CE1 A:HIS112 3.0 21.8 1.0 CD2 A:HIS112 3.0 19.5 1.0 CD2 A:HIS108 3.1 22.0 1.0 ND1 A:HIS112 4.1 22.9 1.0 ND1 A:HIS108 4.1 19.5 1.0 CG A:GLU189 4.1 24.4 1.0 CG A:HIS112 4.2 18.9 1.0 CG A:HIS108 4.2 18.8 1.0 NE2 A:GLN111 4.4 24.3 1.0 CE1 A:TYR831 4.5 25.1 1.0 OE1 A:GLN111 4.6 23.5 1.0 CB A:GLU189 4.7 20.2 1.0 OH A:TYR831 4.7 28.6 1.0 CD A:GLN111 4.9 20.2 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Ide-Bradykinin Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Ide-Bradykinin Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn2001 b:25.2 occ:1.00 NE2 B:HIS112 2.0 22.1 1.0 NE2 B:HIS108 2.0 19.9 1.0 OE1 B:GLU189 2.1 22.9 1.0 CD B:GLU189 2.8 24.7 1.0 OE2 B:GLU189 2.8 24.7 1.0 CE1 B:HIS108 2.9 19.8 1.0 CE1 B:HIS112 3.0 22.6 1.0 CD2 B:HIS112 3.0 19.8 1.0 CD2 B:HIS108 3.1 21.6 1.0 ND1 B:HIS108 4.1 21.6 1.0 ND1 B:HIS112 4.1 23.1 1.0 CG B:HIS112 4.1 22.9 1.0 CG B:HIS108 4.2 20.8 1.0 CG B:GLU189 4.3 23.3 1.0 CE1 B:TYR831 4.4 23.8 1.0 NE2 B:GLN111 4.4 21.6 1.0 OE1 B:GLN111 4.7 23.1 1.0 CB B:GLU189 4.8 21.8 1.0 OH B:TYR831 4.8 28.1 1.0 CD B:GLN111 5.0 22.4 1.0 CG2 B:VAL186 5.0 20.8 1.0

E.Malito, L.A.Ralat, M.Manolopoulou, J.L.Tsay, N.L.Wadlington, W.J.Tang. Molecular Bases For the Recognition of Short Peptide Substrates and Cysteine-Directed Modifications of Human Insulin-Degrading Enzyme Biochemistry V. 47 12822 2008.
ISSN: ISSN 0006-2960
PubMed: 18986166
DOI: 10.1021/BI801192H