Zinc in PDB 1kjz: Structure of the Large Gamma Subunit of Initiation Factor EIF2 From Pyrococcus Abyssi-G235D Mutant

The structure of Structure of the Large Gamma Subunit of Initiation Factor EIF2 From Pyrococcus Abyssi-G235D Mutant, PDB code: 1kjz was solved by E.Schmitt, S.Blanquet, Y.Mechulam, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.00 / 1.85
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	51.480, 86.741, 58.083, 90.00, 110.40, 90.00
R / Rfree (%)	22.5 / 25.5

The binding sites of Zinc atom in the Structure of the Large Gamma Subunit of Initiation Factor EIF2 From Pyrococcus Abyssi-G235D Mutant (pdb code 1kjz). 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 Structure of the Large Gamma Subunit of Initiation Factor EIF2 From Pyrococcus Abyssi-G235D Mutant, PDB code: 1kjz:

Zinc binding site 1 out of 1 in the Structure of the Large Gamma Subunit of Initiation Factor EIF2 From Pyrococcus Abyssi-G235D Mutant


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 Large Gamma Subunit of Initiation Factor EIF2 From Pyrococcus Abyssi-G235D Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn411 b:34.2 occ:1.00 SG A:CYS60 2.2 35.8 1.0 SG A:CYS63 2.3 38.7 1.0 SG A:CYS75 2.3 34.0 1.0 SG A:CYS72 2.4 33.0 1.0 CB A:CYS60 3.1 36.5 1.0 CB A:CYS72 3.2 32.0 1.0 CB A:CYS75 3.4 36.1 1.0 CB A:CYS63 3.4 40.5 1.0 N A:CYS63 3.8 41.5 1.0 N A:CYS75 3.8 35.3 1.0 CA A:CYS75 4.2 35.1 1.0 CA A:CYS63 4.2 38.8 1.0 CA A:CYS60 4.5 37.5 1.0 CB A:ASN62 4.6 45.3 1.0 CA A:CYS72 4.7 31.6 1.0 C A:TYR74 4.7 35.2 1.0 O A:HOH1032 4.8 30.7 1.0 CB A:TYR74 4.8 34.0 1.0 C A:CYS75 4.8 36.1 1.0 N A:GLY76 4.8 35.5 1.0 CB A:HIS77 4.8 41.6 1.0 C A:ASN62 4.9 43.6 1.0 C A:CYS63 4.9 37.5 1.0 N A:HIS77 4.9 36.7 1.0

E.Schmitt, S.Blanquet, Y.Mechulam. The Large Subunit of Initiation Factor AIF2 Is A Close Structural Homologue of Elongation Factors. Embo J. V. 21 1821 2002.
ISSN: ISSN 0261-4189
PubMed: 11927566
DOI: 10.1093/EMBOJ/21.7.1821