Zinc in PDB 4czw: Structure of the Neurospora Crassa PAN2 Catalytic Unit (Protease and Nuclease Domain)

All present enzymatic activity of Structure of the Neurospora Crassa PAN2 Catalytic Unit (Protease and Nuclease Domain):
3.1.13.4;

The structure of Structure of the Neurospora Crassa PAN2 Catalytic Unit (Protease and Nuclease Domain), PDB code: 4czw was solved by M.Christie, E.Izaurralde, O.Weichenrieder, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.14 / 2.60
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	85.565, 85.565, 471.793, 90.00, 90.00, 120.00
R / Rfree (%)	20.86 / 25.35

The binding sites of Zinc atom in the Structure of the Neurospora Crassa PAN2 Catalytic Unit (Protease and Nuclease Domain) (pdb code 4czw). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of the Neurospora Crassa PAN2 Catalytic Unit (Protease and Nuclease Domain), PDB code: 4czw:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of the Neurospora Crassa PAN2 Catalytic Unit (Protease and Nuclease Domain)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of the Neurospora Crassa PAN2 Catalytic Unit (Protease and Nuclease Domain) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn3094 b:47.1 occ:1.00 NE2 A:HIS525 2.0 41.9 1.0 SG A:CYS535 2.3 45.0 1.0 SG A:CYS538 2.3 49.4 1.0 SG A:CYS530 2.3 43.9 1.0 CD2 A:HIS525 3.0 46.4 1.0 CE1 A:HIS525 3.0 39.1 1.0 CB A:CYS530 3.3 42.5 1.0 CB A:CYS538 3.5 42.8 1.0 CB A:CYS535 3.6 44.2 1.0 ND1 A:HIS525 4.0 42.9 1.0 N A:CYS538 4.0 50.7 1.0 CG A:HIS525 4.1 40.6 1.0 NZ A:LYS985 4.2 42.7 1.0 CA A:CYS538 4.2 48.3 1.0 CB A:ALA532 4.7 32.4 1.0 CA A:CYS530 4.7 44.9 1.0 CE A:LYS985 4.9 49.9 1.0 CA A:CYS535 4.9 40.6 1.0 O A:CYS535 4.9 48.8 1.0

Zinc binding site 2 out of 2 in the Structure of the Neurospora Crassa PAN2 Catalytic Unit (Protease and Nuclease Domain)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of the Neurospora Crassa PAN2 Catalytic Unit (Protease and Nuclease Domain) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn3095 b:66.2 occ:1.00 SG A:CYS648 2.2 61.5 1.0 SG A:CYS700 2.3 68.3 1.0 SG A:CYS703 2.3 83.5 1.0 SG A:CYS645 2.3 66.8 1.0 CB A:CYS645 3.1 60.6 1.0 CB A:CYS700 3.1 52.6 1.0 CB A:CYS648 3.6 74.7 1.0 CB A:CYS703 3.7 85.7 1.0 N A:CYS703 3.9 73.7 1.0 N A:CYS648 3.9 71.2 1.0 CA A:CYS648 4.3 68.5 1.0 CA A:CYS703 4.4 85.8 1.0 CG A:GLN707 4.4 67.6 1.0 CB A:LYS702 4.5 72.6 1.0 CA A:CYS700 4.6 60.6 1.0 CA A:CYS645 4.6 65.7 1.0 CB A:HIS647 4.7 68.5 1.0 CB A:HIS650 4.7 64.7 1.0 C A:CYS648 4.9 71.4 1.0 C A:LYS702 4.9 77.5 1.0 NE2 A:GLN707 4.9 68.6 1.0 C A:CYS700 5.0 65.5 1.0

S.Jonas, M.Christie, D.Peter, D.Bhandari, B.Loh, E.Huntzinger, O.Weichenrieder, E.Izaurralde. An Asymmetric PAN3 Dimer Recruits A Single PAN2 Exonuclease to Mediate Mrna Deadenylation and Decay. Nat.Struct.Mol.Biol. V. 21 599 2014.
ISSN: ISSN 1545-9993
PubMed: 24880343
DOI: 10.1038/NSMB.2837