Zinc in PDB 1jml: Conversion of Monomeric Protein L to An Obligate Dimer By Computational Protein Design

The structure of Conversion of Monomeric Protein L to An Obligate Dimer By Computational Protein Design, PDB code: 1jml was solved by J.W.O'neill, B.Kuhlman, D.E.Kim, K.Y.J.Zhang, D.Baker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	23.59 / 1.90
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	46.762, 76.744, 59.797, 90.00, 90.00, 90.00
R / Rfree (%)	19.3 / 21.8

The binding sites of Zinc atom in the Conversion of Monomeric Protein L to An Obligate Dimer By Computational Protein Design (pdb code 1jml). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Conversion of Monomeric Protein L to An Obligate Dimer By Computational Protein Design, PDB code: 1jml:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the Conversion of Monomeric Protein L to An Obligate Dimer By Computational Protein Design


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Conversion of Monomeric Protein L to An Obligate Dimer By Computational Protein Design within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn101 b:25.4 occ:1.00 ND1 A:HIS-3 2.0 21.7 1.0 NE2 A:HIS-5 2.0 25.9 1.0 CD2 A:HIS-5 3.0 26.8 1.0 CE1 A:HIS-3 3.0 22.5 1.0 CG A:HIS-3 3.0 21.4 1.0 CE1 A:HIS-5 3.0 28.6 1.0 CB A:HIS-3 3.4 22.0 1.0 CA A:HIS-3 3.9 21.0 1.0 NE2 A:HIS-3 4.1 21.2 1.0 CG A:HIS-5 4.1 27.4 1.0 ND1 A:HIS-5 4.1 26.7 1.0 CD2 A:HIS-3 4.1 22.4 1.0 N A:HIS-3 4.7 20.1 1.0 O A:HIS-4 4.8 20.9 1.0

Zinc binding site 2 out of 3 in the Conversion of Monomeric Protein L to An Obligate Dimer By Computational Protein Design


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Conversion of Monomeric Protein L to An Obligate Dimer By Computational Protein Design within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn102 b:23.2 occ:1.00 OE2 A:GLU2 2.0 21.7 1.0 ND1 A:HIS-2 2.1 20.2 1.0 OE1 A:GLU27 2.1 24.2 1.0 NE2 A:HIS-4 2.1 20.5 1.0 OE2 A:GLU27 2.7 26.7 1.0 CD A:GLU2 2.7 25.8 1.0 CD A:GLU27 2.7 24.7 1.0 OE1 A:GLU2 2.9 23.0 1.0 CE1 A:HIS-2 3.0 23.3 1.0 CD2 A:HIS-4 3.1 19.7 1.0 CE1 A:HIS-4 3.1 20.2 1.0 CG A:HIS-2 3.2 21.8 1.0 CB A:HIS-2 3.6 20.9 1.0 CA A:HIS-2 3.7 18.8 1.0 CB A:PHE26 3.9 22.9 1.0 CG A:GLU2 4.0 28.9 1.0 NE2 A:HIS-2 4.1 23.2 1.0 ND1 A:HIS-4 4.2 20.4 1.0 CG A:GLU27 4.2 25.3 1.0 CG A:HIS-4 4.2 20.0 1.0 N A:PHE26 4.2 22.8 1.0 CD2 A:HIS-2 4.2 23.1 1.0 N A:GLU27 4.3 23.3 1.0 N A:HIS-1 4.5 21.5 1.0 N A:HIS-2 4.6 18.6 1.0 CA A:PHE26 4.6 22.0 1.0 C A:HIS-2 4.7 20.1 1.0 CB A:THR25 4.9 24.8 1.0 CB A:GLU27 4.9 25.3 1.0 CG A:PHE26 4.9 21.8 1.0 C A:PHE26 5.0 22.8 1.0 CD2 A:PHE26 5.0 22.3 1.0

Zinc binding site 3 out of 3 in the Conversion of Monomeric Protein L to An Obligate Dimer By Computational Protein Design


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Conversion of Monomeric Protein L to An Obligate Dimer By Computational Protein Design within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn103 b:27.0 occ:1.00 NE2 A:HIS-6 2.0 23.6 1.0 OD1 A:ASP50 2.0 22.5 1.0 O A:HOH238 2.3 33.9 1.0 CG A:ASP50 2.9 24.1 1.0 CE1 A:HIS-6 3.0 26.9 1.0 CD2 A:HIS-6 3.0 23.1 1.0 OD2 A:ASP50 3.1 24.6 1.0 O A:VAL51 4.0 21.8 1.0 ND1 A:HIS-6 4.1 26.1 1.0 CG A:HIS-6 4.1 25.6 1.0 CB A:ASP50 4.3 20.9 1.0 N A:VAL51 4.5 19.0 1.0 O A:HOH219 4.6 36.9 1.0 CA A:ASP50 4.7 19.9 1.0 C A:VAL51 4.8 21.2 1.0 C A:ASP50 4.9 19.7 1.0 CG2 A:VAL52 5.0 26.6 1.0

B.Kuhlman, J.W.O'neill, D.E.Kim, K.Y.Zhang, D.Baker. Conversion of Monomeric Protein L to An Obligate Dimer By Computational Protein Design. Proc.Natl.Acad.Sci.Usa V. 98 10687 2001.
ISSN: ISSN 0027-8424
PubMed: 11526208
DOI: 10.1073/PNAS.181354398