Zinc in PDB 1nl5: Engineered High-Affinity Maltose-Binding Protein

The structure of Engineered High-Affinity Maltose-Binding Protein, PDB code: 1nl5 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)	60.80 / 2.10
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	121.590, 121.590, 62.440, 90.00, 90.00, 90.00
R / Rfree (%)	25.2 / 29

The binding sites of Zinc atom in the Engineered High-Affinity Maltose-Binding Protein (pdb code 1nl5). 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 Engineered High-Affinity Maltose-Binding Protein, PDB code: 1nl5:

Zinc binding site 1 out of 1 in the Engineered High-Affinity 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 Engineered High-Affinity Maltose-Binding Protein within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn500 b:41.7 occ:1.00 NE2 A:HIS203 2.1 24.8 1.0 O A:HOH656 2.8 32.3 1.0 CE1 A:HIS203 3.1 27.3 1.0 CD2 A:HIS203 3.2 25.3 1.0 O A:HOH618 3.2 38.1 1.0 CB A:PRO133 3.8 31.1 1.0 CB A:ASN201 4.2 33.0 1.0 OD1 A:ASN201 4.2 36.0 1.0 ND1 A:HIS203 4.2 28.1 1.0 CE A:LYS137 4.3 49.1 1.0 CG A:HIS203 4.3 29.5 1.0 CG A:ASN201 4.5 34.9 1.0 CA A:PRO133 4.6 30.1 1.0 C A:PRO133 4.8 31.5 1.0 O A:PRO133 4.8 29.7 1.0 CG A:PRO133 4.9 30.0 1.0 CD A:LYS137 5.0 45.5 1.0

P.G.Telmer, B.H.Shilton. Insights Into the Conformational Equilibria of Maltose-Binding Protein By Analysis of High Affinity Mutants. J.Biol.Chem. V. 278 34555 2003.
ISSN: ISSN 0021-9258
PubMed: 12794084
DOI: 10.1074/JBC.M301004200