Zinc in PDB 1zjl: Crystal Structure of Zinc-Bound Engineered Maltose Binding Protein

The structure of Crystal Structure of Zinc-Bound Engineered Maltose Binding Protein, PDB code: 1zjl was solved by P.G.Telmer, B.H.Shilton, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.86 / 2.00
Space group	P 32
Cell size a, b, c (Å), α, β, γ (°)	80.500, 80.500, 55.900, 90.00, 90.00, 120.00
R / Rfree (%)	20.4 / 23.2

The binding sites of Zinc atom in the Crystal Structure of Zinc-Bound Engineered Maltose Binding Protein (pdb code 1zjl). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of Zinc-Bound Engineered Maltose Binding Protein, PDB code: 1zjl:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Crystal Structure of Zinc-Bound Engineered Maltose Binding Protein


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 Zinc-Bound Engineered Maltose Binding Protein within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn371 b:43.9 occ:1.00 NE2 A:HIS66 2.1 35.2 1.0 ND1 A:HIS63 2.2 28.1 1.0 O A:HOH658 2.5 40.8 1.0 CD2 A:HIS66 2.8 33.4 1.0 CG A:HIS63 3.0 25.6 1.0 CE1 A:HIS63 3.2 28.1 1.0 CB A:HIS63 3.2 21.7 1.0 CE1 A:HIS66 3.3 34.8 1.0 OD2 A:ASP65 3.9 32.9 1.0 OD1 A:ASP65 3.9 33.4 1.0 CG A:HIS66 4.0 32.5 1.0 CD2 A:HIS63 4.2 28.6 1.0 ND1 A:HIS66 4.2 35.0 1.0 NE2 A:HIS63 4.3 28.5 1.0 CG A:ASP65 4.3 31.0 1.0 NE1 A:TRP62 4.4 32.4 1.0 O A:HOH591 4.6 32.5 1.0 CA A:HIS63 4.7 20.0 1.0 CD1 A:TRP62 4.8 30.2 1.0

Zinc binding site 2 out of 4 in the Crystal Structure of Zinc-Bound Engineered Maltose Binding Protein


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 Zinc-Bound Engineered Maltose Binding Protein within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn372 b:90.5 occ:1.00 O A:LYS1 2.4 36.1 1.0 N A:LYS1 3.1 36.9 1.0 C A:LYS1 3.4 35.2 1.0 CA A:LYS1 3.8 36.5 1.0 CG A:LYS1 4.2 42.1 1.0 OD1 A:ASP55 4.3 34.4 1.0 O A:HOH589 4.4 40.1 1.0 N A:ILE2 4.6 32.1 1.0 CB A:LYS1 4.6 37.9 1.0

Zinc binding site 3 out of 4 in the Crystal Structure of Zinc-Bound Engineered Maltose Binding Protein


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Zinc-Bound Engineered Maltose Binding Protein within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn373 b:50.4 occ:1.00 NE2 A:HIS63 2.0 28.5 1.0 NZ A:LYS15 2.4 16.7 1.0 O A:HOH640 2.5 31.5 1.0 O A:HOH642 2.8 36.2 1.0 CE1 A:HIS63 2.9 28.1 1.0 CE A:LYS15 3.0 13.8 1.0 CD2 A:HIS63 3.1 28.6 1.0 ND1 A:HIS63 4.1 28.1 1.0 CG A:HIS63 4.1 25.6 1.0 CD A:LYS15 4.5 15.9 1.0 O A:HOH641 4.6 34.9 1.0

Zinc binding site 4 out of 4 in the Crystal Structure of Zinc-Bound Engineered Maltose Binding Protein


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Zinc-Bound Engineered Maltose Binding Protein within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn374 b:21.3 occ:1.00 ND1 A:HIS39 2.0 11.0 1.0 O A:HIS39 2.1 12.0 1.0 O A:HOH411 2.2 14.5 1.0 CE1 A:HIS39 3.0 9.3 1.0 CG A:HIS39 3.1 10.0 1.0 C A:HIS39 3.2 12.8 1.0 CB A:HIS39 3.4 8.8 1.0 O A:HOH647 3.4 34.8 1.0 CA A:HIS39 3.9 9.7 1.0 O A:HOH648 4.0 41.3 1.0 O A:HOH475 4.1 16.9 1.0 NE2 A:HIS39 4.1 10.2 1.0 CD2 A:HIS39 4.2 9.8 1.0 N A:PRO40 4.3 14.2 1.0 CA A:GLY13 4.6 12.4 1.0 N A:HIS39 4.6 10.7 1.0 C A:PRO40 4.6 19.6 1.0 CA A:PRO40 4.7 17.1 1.0 O A:PRO40 4.8 20.4 1.0 N A:ASP41 4.9 22.3 1.0 N A:GLY13 4.9 13.8 1.0

P.G.Telmer, B.H.Shilton. Structural Studies of An Engineered Zinc Biosensor Reveal An Unanticipated Mode of Zinc Binding. J.Mol.Biol. V. 354 829 2005.
ISSN: ISSN 0022-2836
PubMed: 16288781
DOI: 10.1016/J.JMB.2005.10.016