Zinc in PDB 7cei: The Endonuclease Domain of Colicin E7 in Complex with Its Inhibitor IM7 Protein

The structure of The Endonuclease Domain of Colicin E7 in Complex with Its Inhibitor IM7 Protein, PDB code: 7cei was solved by T.P.Ko, C.C.Liao, W.Y.Ku, K.F.Chak, H.S.Yuan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 2.30
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	65.440, 76.020, 119.990, 90.00, 90.00, 90.00
R / Rfree (%)	20.3 / 27

The binding sites of Zinc atom in the The Endonuclease Domain of Colicin E7 in Complex with Its Inhibitor IM7 Protein (pdb code 7cei). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the The Endonuclease Domain of Colicin E7 in Complex with Its Inhibitor IM7 Protein, PDB code: 7cei:

Zinc binding site 1 out of 1 in the The Endonuclease Domain of Colicin E7 in Complex with Its Inhibitor IM7 Protein


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Endonuclease Domain of Colicin E7 in Complex with Its Inhibitor IM7 Protein within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn600 b:51.0 occ:1.00 NE2 B:HIS569 1.9 43.0 1.0 ND1 B:HIS544 2.1 44.5 1.0 O B:HOH863 2.2 21.2 1.0 CE1 B:HIS544 2.4 44.5 1.0 NE2 B:HIS573 2.6 48.6 1.0 CE1 B:HIS569 2.7 42.9 1.0 CE1 B:HIS573 2.9 48.0 1.0 CD2 B:HIS569 3.1 43.0 1.0 CG B:HIS544 3.2 43.6 1.0 NE2 B:HIS544 3.5 44.6 1.0 ND1 B:HIS569 3.8 42.4 1.0 CD2 B:HIS544 3.9 43.7 1.0 CD2 B:HIS573 3.9 48.8 1.0 CB B:HIS544 4.0 41.6 1.0 CG B:HIS569 4.1 43.0 1.0 N B:HIS545 4.1 41.8 1.0 ND1 B:HIS573 4.2 48.5 1.0 CA B:HIS544 4.2 40.5 1.0 O B:HOH798 4.5 50.2 1.0 CG B:HIS573 4.7 49.2 1.0 O B:HIS545 4.7 44.1 1.0 C B:HIS544 4.7 41.1 1.0

T.P.Ko, C.C.Liao, W.Y.Ku, K.F.Chak, H.S.Yuan. The Crystal Structure of the Dnase Domain of Colicin E7 in Complex with Its Inhibitor IM7 Protein. Structure Fold.Des. V. 7 91 1999.
ISSN: ISSN 0969-2126
PubMed: 10368275
DOI: 10.1016/S0969-2126(99)80012-4