Zinc in PDB 4k87: Crystal Structure of Human Prolyl-Trna Synthetase (Substrate Bound Form)

All present enzymatic activity of Crystal Structure of Human Prolyl-Trna Synthetase (Substrate Bound Form):
6.1.1.15;

The structure of Crystal Structure of Human Prolyl-Trna Synthetase (Substrate Bound Form), PDB code: 4k87 was solved by K.Y.Hwang, J.H.Son, E.H.Lee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.98 / 2.30
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	120.163, 120.163, 107.098, 90.00, 90.00, 120.00
R / Rfree (%)	21.7 / 26.7

The binding sites of Zinc atom in the Crystal Structure of Human Prolyl-Trna Synthetase (Substrate Bound Form) (pdb code 4k87). 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 Crystal Structure of Human Prolyl-Trna Synthetase (Substrate Bound Form), PDB code: 4k87:

Zinc binding site 1 out of 1 in the Crystal Structure of Human Prolyl-Trna Synthetase (Substrate Bound Form)


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 Human Prolyl-Trna Synthetase (Substrate Bound Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:87.8 occ:1.00 SG A:CYS453 2.1 70.3 1.0 SG A:CYS495 2.3 78.4 1.0 SG A:CYS448 2.6 81.2 1.0 SG A:CYS497 2.6 98.7 1.0 CB A:CYS453 3.1 70.0 1.0 CB A:CYS495 3.4 81.3 1.0 CB A:CYS497 3.4 91.0 1.0 CB A:CYS448 3.5 89.9 1.0 N A:CYS448 4.0 83.0 1.0 CE1 A:PHE447 4.1 78.6 1.0 CD1 A:PHE447 4.2 71.7 1.0 N A:CYS497 4.3 90.4 1.0 CA A:CYS448 4.4 85.7 1.0 CA A:CYS453 4.5 79.3 1.0 CA A:CYS497 4.5 93.9 1.0 OD1 A:ASN500 4.6 93.7 1.0 CA A:CYS495 4.8 83.8 1.0 N A:VAL496 4.9 85.8 1.0 C A:CYS495 5.0 85.2 1.0

J.Son, E.H.Lee, M.Park, J.H.Kim, J.Kim, S.Kim, Y.H.Jeon, K.Y.Hwang. Conformational Changes in Human Prolyl-Trna Synthetase Upon Binding of the Substrates Proline and Atp and the Inhibitor Halofuginone Acta Crystallogr.,Sect.D V. 69 2136 2013.
ISSN: ISSN 0907-4449
DOI: 10.1107/S0907444913020556