Zinc in PDB 3hay: Crystal Structure of A Substrate-Bound Full H/Aca Rnp From Pyrococcus Furiosus

The structure of Crystal Structure of A Substrate-Bound Full H/Aca Rnp From Pyrococcus Furiosus, PDB code: 3hay was solved by K.Ye, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 4.99
Space group	P 64 2 2
Cell size a, b, c (Å), α, β, γ (°)	189.518, 189.518, 279.045, 90.00, 90.00, 120.00
R / Rfree (%)	32.3 / 36.7

The structure of Crystal Structure of A Substrate-Bound Full H/Aca Rnp From Pyrococcus Furiosus also contains other interesting chemical elements:

Fluorine

(F)

1 atom

The binding sites of Zinc atom in the Crystal Structure of A Substrate-Bound Full H/Aca Rnp From Pyrococcus Furiosus (pdb code 3hay). 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 A Substrate-Bound Full H/Aca Rnp From Pyrococcus Furiosus, PDB code: 3hay:

Zinc binding site 1 out of 1 in the Crystal Structure of A Substrate-Bound Full H/Aca Rnp From Pyrococcus Furiosus


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 A Substrate-Bound Full H/Aca Rnp From Pyrococcus Furiosus within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn201 b:0.3 occ:1.00 SG C:CYS23 2.4 0.9 1.0 SG C:CYS8 2.4 0.3 1.0 SG C:CYS11 2.4 0.1 1.0 SG C:CYS20 2.4 0.6 1.0 CB C:CYS8 3.4 0.9 1.0 CB C:CYS23 3.4 0.7 1.0 CB C:CYS11 3.5 0.5 1.0 CB C:CYS20 3.5 0.4 1.0 N C:CYS23 4.0 0.6 1.0 N C:CYS11 4.3 0.3 1.0 CA C:CYS23 4.3 0.6 1.0 CA C:CYS11 4.5 0.5 1.0 CB C:GLU25 4.7 0.1 1.0 N C:GLY24 4.7 0.5 1.0 CB C:LYS10 4.8 0.1 1.0 CA C:CYS8 4.8 0.7 1.0 CA C:CYS20 4.9 0.3 1.0 N C:GLU25 4.9 0.1 1.0 CB C:VAL22 5.0 0.6 1.0 C C:CYS23 5.0 0.6 1.0

J.Duan, L.Li, J.Lu, W.Wang, K.Ye. Structural Mechanism of Substrate Rna Recruitment in H/Aca Rna-Guided Pseudouridine Synthase. Mol.Cell V. 34 427 2009.
ISSN: ISSN 1097-2765
PubMed: 19481523
DOI: 10.1016/J.MOLCEL.2009.05.005