Zinc in PDB 4hvc: Crystal Structure of Human Prolyl-Trna Synthetase in Complex with Halofuginone and Atp Analogue

All present enzymatic activity of Crystal Structure of Human Prolyl-Trna Synthetase in Complex with Halofuginone and Atp Analogue:
6.1.1.15; 6.1.1.17;

The structure of Crystal Structure of Human Prolyl-Trna Synthetase in Complex with Halofuginone and Atp Analogue, PDB code: 4hvc was solved by H.Zhou, L.Sun, X.L.Yang, P.Schimmel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.43 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	72.544, 93.100, 87.004, 90.00, 107.95, 90.00
R / Rfree (%)	20.4 / 22.7

The structure of Crystal Structure of Human Prolyl-Trna Synthetase in Complex with Halofuginone and Atp Analogue also contains other interesting chemical elements:

Bromine	(Br)	2 atoms
Magnesium	(Mg)	2 atoms
Chlorine	(Cl)	2 atoms

The binding sites of Zinc atom in the Crystal Structure of Human Prolyl-Trna Synthetase in Complex with Halofuginone and Atp Analogue (pdb code 4hvc). 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 Human Prolyl-Trna Synthetase in Complex with Halofuginone and Atp Analogue, PDB code: 4hvc:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Human Prolyl-Trna Synthetase in Complex with Halofuginone and Atp Analogue


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 in Complex with Halofuginone and Atp Analogue within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1604 b:73.1 occ:1.00 SG A:CYS1453 2.1 80.8 1.0 SG A:CYS1495 2.5 82.1 1.0 SG A:CYS1448 2.6 80.3 1.0 CB A:CYS1497 2.8 88.6 1.0 CB A:CYS1453 3.1 80.9 1.0 SG A:CYS1497 3.2 88.6 1.0 CA A:CYS1497 3.6 89.0 1.0 N A:CYS1497 3.7 87.6 1.0 CB A:CYS1495 3.8 85.7 1.0 CB A:CYS1448 3.9 80.2 1.0 N A:CYS1448 4.2 76.1 1.0 CE1 A:PHE1447 4.2 72.7 1.0 CD1 A:PHE1447 4.3 72.3 1.0 CA A:CYS1453 4.5 81.4 1.0 CA A:CYS1448 4.7 77.9 1.0 N A:VAL1496 4.9 85.7 1.0 C A:VAL1496 4.9 88.3 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Human Prolyl-Trna Synthetase in Complex with Halofuginone and Atp Analogue


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 Human Prolyl-Trna Synthetase in Complex with Halofuginone and Atp Analogue within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1604 b:65.7 occ:1.00 SG B:CYS1495 2.1 67.8 1.0 SG B:CYS1453 2.3 68.9 1.0 SG B:CYS1448 2.4 65.1 1.0 CB B:CYS1497 2.8 74.8 1.0 CB B:CYS1495 3.2 70.8 1.0 CB B:CYS1453 3.3 69.0 1.0 SG B:CYS1497 3.4 76.7 1.0 CB B:CYS1448 3.4 65.2 1.0 N B:CYS1497 3.8 74.2 1.0 CA B:CYS1497 3.8 75.9 1.0 N B:CYS1448 3.8 62.6 1.0 CA B:CYS1448 4.2 63.6 1.0 CD1 B:PHE1447 4.3 59.7 1.0 CE1 B:PHE1447 4.4 58.9 1.0 CA B:CYS1495 4.6 71.6 1.0 ND2 B:ASN1500 4.7 74.7 1.0 CA B:CYS1453 4.7 69.3 1.0 N B:VAL1496 4.8 71.8 1.0 C B:CYS1495 4.9 72.8 1.0 CB B:ASN1500 4.9 74.2 1.0 C B:VAL1496 4.9 74.5 1.0 C B:PHE1447 5.0 61.5 1.0

H.Zhou, L.Sun, X.L.Yang, P.Schimmel. Atp-Directed Capture of Bioactive Herbal-Based Medicine on Human Trna Synthetase. Nature V. 494 121 2012.
ISSN: ISSN 0028-0836
PubMed: 23263184
DOI: 10.1038/NATURE11774