Zinc in PDB 1ef0: Crystal Structure of Pi-Scei Miniprecursor

All present enzymatic activity of Crystal Structure of Pi-Scei Miniprecursor:
3.6.1.34;

The structure of Crystal Structure of Pi-Scei Miniprecursor, PDB code: 1ef0 was solved by B.W.Poland, M.-Q.Xu, F.A.Quiocho, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	59.003, 101.683, 86.765, 90.00, 93.51, 90.00
R / Rfree (%)	23.1 / 28.1

The binding sites of Zinc atom in the Crystal Structure of Pi-Scei Miniprecursor (pdb code 1ef0). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Crystal Structure of Pi-Scei Miniprecursor, PDB code: 1ef0:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the Crystal Structure of Pi-Scei Miniprecursor


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 Pi-Scei Miniprecursor within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn701 b:13.4 occ:0.25 ZN A:ZN701 0.0 13.4 0.2 SG A:CYS455 1.8 28.8 0.2 O A:HOH875 2.1 34.9 0.2 ND1 A:HIS442 2.3 30.8 0.2 ND1 A:HIS442 2.4 30.5 0.5 NE2 A:HIS453 2.4 24.0 0.2 ZN A:ZN701 2.4 42.7 0.2 CE1 A:HIS453 2.4 23.5 0.5 CE1 A:HIS453 2.5 23.9 0.2 NE2 A:HIS453 2.6 23.3 0.5 CE1 A:HIS442 3.3 31.0 0.2 CG A:HIS442 3.3 30.8 0.2 CE1 A:HIS442 3.4 30.8 0.5 CG A:HIS442 3.4 30.4 0.5 CB A:HIS442 3.6 30.6 0.2 CB A:HIS442 3.6 30.3 0.5 CB A:CYS455 3.6 28.6 0.2 ND1 A:HIS453 3.7 23.7 0.5 CD2 A:HIS453 3.8 23.9 0.2 ND1 A:HIS453 3.8 23.9 0.2 CD2 A:HIS453 4.0 23.5 0.5 NE2 A:HIS442 4.5 30.9 0.2 OE1 A:GLU80 4.5 18.8 0.2 CG A:HIS453 4.5 24.0 0.2 CD2 A:HIS442 4.5 30.8 0.2 NE2 A:HIS442 4.5 30.6 0.5 CG A:HIS453 4.5 23.6 0.5 CD2 A:HIS442 4.5 30.4 0.5 O A:ALA454 4.5 28.2 1.0 SG A:CYS455 4.5 30.8 0.5 CA A:CYS455 4.6 29.1 0.5 OE1 A:GLU80 4.6 22.0 0.5 CA A:CYS455 4.6 28.6 0.2

Zinc binding site 2 out of 3 in the Crystal Structure of Pi-Scei Miniprecursor


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 Pi-Scei Miniprecursor within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn701 b:42.7 occ:0.25 ZN A:ZN701 0.0 42.7 0.2 SG A:CYS455 2.4 28.8 0.2 NE2 A:HIS453 2.4 23.3 0.5 ZN A:ZN701 2.4 13.4 0.2 OE1 A:GLU80 2.5 22.0 0.5 OE1 A:GLU80 2.8 18.8 0.2 CE1 A:HIS453 2.8 23.9 0.2 SG A:CYS455 3.1 30.8 0.5 O A:HOH875 3.2 19.4 0.5 NE2 A:HIS453 3.2 24.0 0.2 CB A:CYS455 3.2 28.6 0.2 CE1 A:HIS453 3.3 23.5 0.5 CD2 A:HIS453 3.5 23.5 0.5 CD A:GLU80 3.6 21.1 0.5 CD A:GLU80 3.7 19.0 0.2 ND1 A:HIS453 3.8 23.9 0.2 O A:HOH875 3.8 34.9 0.2 OE2 A:GLU80 3.9 21.4 0.5 OE2 A:GLU80 4.3 19.0 0.2 CD2 A:HIS453 4.3 23.9 0.2 CB A:CYS455 4.4 29.2 0.5 ND1 A:HIS453 4.5 23.7 0.5 CG A:HIS453 4.6 23.6 0.5 CG A:HIS453 4.6 24.0 0.2 ND1 A:HIS442 4.6 30.8 0.2 CA A:CYS455 4.6 29.1 0.5 CG A:GLU80 4.7 19.2 0.2 CA A:CYS455 4.7 28.6 0.2 ND1 A:HIS442 4.7 30.5 0.5 CG A:GLU80 4.9 20.8 0.5

Zinc binding site 3 out of 3 in the Crystal Structure of Pi-Scei Miniprecursor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Pi-Scei Miniprecursor within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn701 b:18.6 occ:1.00 OE2 B:GLU80 2.2 23.3 1.0 O B:HOH719 2.4 13.7 1.0 NE2 B:HIS453 2.5 19.3 1.0 SG B:CYS455 2.5 29.3 1.0 CD B:GLU80 3.0 22.5 1.0 OE1 B:GLU80 3.1 23.6 1.0 CD2 B:HIS453 3.3 18.4 1.0 CB B:CYS455 3.5 26.7 1.0 CE1 B:HIS453 3.5 19.2 1.0 CA B:CYS455 3.7 27.1 1.0 O B:HOH841 4.0 35.6 1.0 N B:CYS455 4.1 25.1 1.0 CG B:GLU80 4.3 21.3 1.0 CG B:HIS453 4.5 19.2 1.0 ND1 B:HIS453 4.6 18.7 1.0 C B:ALA454 4.9 23.9 1.0 CB B:GLU80 5.0 18.8 1.0

B.W.Poland, M.Q.Xu, F.A.Quiocho. Structural Insights Into the Protein Splicing Mechanism of Pi-Scei. J.Biol.Chem. V. 275 16408 2000.
ISSN: ISSN 0021-9258
PubMed: 10828056
DOI: 10.1074/JBC.275.22.16408