Zinc in PDB 3hfy: Mutant of Trna-Guanine Transglycosylase (K52M)

All present enzymatic activity of Mutant of Trna-Guanine Transglycosylase (K52M):
2.4.2.29;

The structure of Mutant of Trna-Guanine Transglycosylase (K52M), PDB code: 3hfy was solved by T.Ritschel, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.00
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	84.600, 65.200, 71.600, 90.00, 93.70, 90.00
R / Rfree (%)	20.4 / 27.8

The binding sites of Zinc atom in the Mutant of Trna-Guanine Transglycosylase (K52M) (pdb code 3hfy). 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 Mutant of Trna-Guanine Transglycosylase (K52M), PDB code: 3hfy:

Zinc binding site 1 out of 1 in the Mutant of Trna-Guanine Transglycosylase (K52M)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Mutant of Trna-Guanine Transglycosylase (K52M) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn400 b:39.3 occ:1.00 SG A:CYS320 2.2 36.8 1.0 SG A:CYS323 2.3 36.7 1.0 SG A:CYS318 2.3 40.9 1.0 ND1 A:HIS349 2.4 25.1 1.0 CB A:CYS320 2.9 33.0 1.0 CB A:CYS323 3.1 44.2 1.0 CE1 A:HIS349 3.2 22.4 1.0 CB A:CYS318 3.2 35.9 1.0 CG A:HIS349 3.5 17.5 1.0 CB A:HIS349 3.9 26.6 1.0 N A:CYS323 3.9 51.0 1.0 CA A:CYS320 4.0 34.6 1.0 N A:CYS320 4.1 39.2 1.0 CA A:CYS323 4.1 52.3 1.0 CA A:HIS349 4.1 19.9 1.0 NE2 A:HIS349 4.4 23.1 1.0 C A:CYS320 4.4 37.1 1.0 O A:CYS320 4.5 50.0 1.0 CD2 A:HIS349 4.6 18.3 1.0 CA A:CYS318 4.6 45.6 1.0 O A:HIS349 4.6 21.6 1.0 CB A:LEU314 4.7 37.2 1.0 C A:CYS318 4.8 48.0 1.0 C A:HIS349 4.8 20.8 1.0 CB A:VAL322 4.9 39.2 1.0 O A:CYS318 4.9 59.0 1.0

T.Ritschel, C.Atmanene, K.Reuter, A.Van Dorsselaer, S.Sanglier-Cianferani, G.Klebe. An Integrative Approach Combining Noncovalent Mass Spectrometry, Enzyme Kinetics and X-Ray Crystallography to Decipher Tgt Protein-Protein and Protein-Rna Interaction J.Mol.Biol. V. 393 833 2009.
ISSN: ISSN 0022-2836
PubMed: 19627989
DOI: 10.1016/J.JMB.2009.07.040