Zinc in PDB 1zin: Adenylate Kinase with Bound AP5A

All present enzymatic activity of Adenylate Kinase with Bound AP5A:
2.7.4.3;

The structure of Adenylate Kinase with Bound AP5A, PDB code: 1zin was solved by M.B.Berry, G.N.Phillips Jr., with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.60
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	41.170, 62.338, 41.600, 90.00, 116.74, 90.00
R / Rfree (%)	17.3 / 21.6

The binding sites of Zinc atom in the Adenylate Kinase with Bound AP5A (pdb code 1zin). 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 Adenylate Kinase with Bound AP5A, PDB code: 1zin:

Zinc binding site 1 out of 1 in the Adenylate Kinase with Bound AP5A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Adenylate Kinase with Bound AP5A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn219 b:17.1 occ:1.00 SG A:CYS133 2.3 19.4 1.0 SG A:CYS150 2.3 13.5 1.0 SG A:CYS153 2.3 15.8 1.0 SG A:CYS130 2.3 14.5 1.0 CB A:CYS130 3.1 12.6 1.0 CB A:CYS150 3.1 14.0 1.0 CB A:CYS133 3.3 19.7 1.0 CB A:CYS153 3.6 14.1 1.0 N A:CYS133 3.6 23.5 1.0 N A:CYS153 3.8 13.8 1.0 CA A:CYS133 4.0 21.6 1.0 CA A:CYS153 4.2 14.5 1.0 CB A:LYS152 4.4 20.9 1.0 N A:GLY155 4.4 13.5 1.0 CB A:ASN132 4.5 33.3 1.0 CB A:ALA135 4.6 14.7 1.0 CA A:CYS130 4.6 12.5 1.0 CA A:CYS150 4.6 13.3 1.0 C A:CYS133 4.7 21.1 1.0 CA A:GLY155 4.7 17.7 1.0 C A:ASN132 4.7 23.9 1.0 N A:GLY134 4.8 18.7 1.0 C A:LYS152 4.8 16.1 1.0 N A:ALA135 4.8 14.1 1.0 C A:CYS153 4.8 14.3 1.0 N A:GLY154 4.9 13.2 1.0 CA A:ASN132 5.0 22.9 1.0 CA A:LYS152 5.0 16.1 1.0

M.B.Berry, G.N.Phillips Jr.. Crystal Structures of Bacillus Stearothermophilus Adenylate Kinase with Bound AP5A, MG2+ AP5A, and MN2+ AP5A Reveal An Intermediate Lid Position and Six Coordinate Octahedral Geometry For Bound MG2+ and MN2+. Proteins V. 32 276 1998.
ISSN: ISSN 0887-3585
PubMed: 9715904
DOI: 10.1002/(SICI)1097-0134(19980815)32:3<276::AID-PROT3>3.0.CO;2-G