Zinc in PDB 4typ: Crystal Structure of An Adenylate Kinase Mutant--AKM1

All present enzymatic activity of Crystal Structure of An Adenylate Kinase Mutant--AKM1:
2.7.4.3;

The structure of Crystal Structure of An Adenylate Kinase Mutant--AKM1, PDB code: 4typ was solved by S.Moon, E.Bae, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	43.641, 123.338, 86.693, 90.00, 98.28, 90.00
R / Rfree (%)	28.8 / 32.9

The binding sites of Zinc atom in the Crystal Structure of An Adenylate Kinase Mutant--AKM1 (pdb code 4typ). 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 An Adenylate Kinase Mutant--AKM1, PDB code: 4typ:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of An Adenylate Kinase Mutant--AKM1


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 An Adenylate Kinase Mutant--AKM1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn301 b:0.3 occ:1.00 OD2 B:ASP153 1.8 48.9 1.0 SG B:CYS130 2.0 40.9 1.0 SG B:CYS133 2.1 42.9 1.0 SG B:CYS150 2.2 53.4 1.0 CG B:ASP153 2.8 51.0 1.0 CB B:CYS130 3.0 41.0 1.0 OD1 B:ASP153 3.1 51.2 1.0 CB B:CYS150 3.4 54.5 1.0 CB B:CYS133 3.4 42.0 1.0 N B:CYS133 3.7 41.1 1.0 CG2 B:THR135 3.8 46.4 1.0 CA B:CYS133 4.1 41.4 1.0 CB B:ASP153 4.1 52.5 1.0 CA B:CYS130 4.5 41.0 1.0 CB B:VAL132 4.5 42.3 1.0 N B:ASP153 4.5 52.8 1.0 N B:GLY134 4.6 42.8 1.0 C B:CYS133 4.8 41.6 1.0 N B:THR135 4.8 43.3 1.0 CB B:THR135 4.8 45.8 1.0 CA B:CYS150 4.8 55.1 1.0 C B:VAL132 4.8 40.8 1.0 CB B:LYS152 4.9 54.2 1.0 CA B:ASP153 4.9 53.3 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of An Adenylate Kinase Mutant--AKM1


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 An Adenylate Kinase Mutant--AKM1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:0.5 occ:1.00 SG A:CYS150 1.7 73.6 1.0 SG A:CYS130 1.9 64.8 1.0 OD2 A:ASP153 2.3 85.9 1.0 CB A:CYS150 2.6 77.1 1.0 OD1 A:ASP153 2.7 86.2 1.0 CB A:CYS130 2.8 66.1 1.0 CG A:ASP153 2.8 87.6 1.0 SG A:CYS133 2.9 74.8 1.0 CA A:CYS150 4.1 79.9 1.0 CG2 A:THR135 4.2 61.0 1.0 N A:CYS133 4.2 74.6 1.0 CA A:CYS130 4.3 67.1 1.0 CB A:CYS133 4.3 74.3 1.0 CB A:ASP153 4.3 88.9 1.0 N A:GLY155 4.5 76.1 1.0 CB A:VAL132 4.5 73.0 1.0 N A:ASP153 4.7 93.8 1.0 N A:GLY154 4.8 80.7 1.0 CA A:CYS133 4.8 74.2 1.0 O A:GLY155 4.9 73.0 1.0 CA A:GLY155 4.9 74.7 1.0 C A:CYS150 4.9 82.2 1.0 N A:ASP151 4.9 84.4 1.0 C A:CYS130 4.9 69.6 1.0 N A:VAL132 4.9 74.7 1.0 N A:CYS150 5.0 81.2 1.0

S.Moon, E.Bae. Crystal Structures of Thermally Stable Adenylate Kinase Mutants Designed By Local Structural Entropy Optimization and Structure-Guided Mutagenesis J Korean Soc Appl Biol Chem V. 57 661 2014.
ISSN: ISSN 1738-2203
DOI: 10.1007/S13765-014-4228-4