Zinc in PDB 1gle: Cation Promoted Association (Cpa) of A Regulatory and Target Protein Is Controlled By Phosphorylation

All present enzymatic activity of Cation Promoted Association (Cpa) of A Regulatory and Target Protein Is Controlled By Phosphorylation:
2.7.1.30; 2.7.1.69;

The structure of Cation Promoted Association (Cpa) of A Regulatory and Target Protein Is Controlled By Phosphorylation, PDB code: 1gle was solved by M.D.Feese, N.D.Meadow, S.Roseman, D.W.Pettigrew, S.J.Remington, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	21.80 / 2.94
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	124.030, 125.110, 133.330, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Zinc atom in the Cation Promoted Association (Cpa) of A Regulatory and Target Protein Is Controlled By Phosphorylation (pdb code 1gle). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Cation Promoted Association (Cpa) of A Regulatory and Target Protein Is Controlled By Phosphorylation, PDB code: 1gle:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Cation Promoted Association (Cpa) of A Regulatory and Target Protein Is Controlled By Phosphorylation


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Cation Promoted Association (Cpa) of A Regulatory and Target Protein Is Controlled By Phosphorylation within 5.0Å range: probe atom residue distance (Å) B Occ F:Zn169 b:33.9 occ:1.00 OE2 G:GLU478 1.9 11.4 1.0 NE2 F:HIS75 2.0 51.3 1.0 O F:HOH175 2.0 5.8 1.0 NE2 F:HIS90 2.2 20.4 1.0 CE1 F:HIS75 2.7 48.7 1.0 CD G:GLU478 2.8 69.8 1.0 CD2 F:HIS75 3.0 57.1 1.0 CE1 F:HIS90 3.0 20.4 1.0 CD2 F:HIS90 3.3 16.0 1.0 OE1 G:GLU478 3.3 43.1 1.0 CG1 F:VAL96 3.6 43.0 1.0 CB F:VAL96 3.6 47.0 1.0 N F:VAL96 3.7 51.8 1.0 ND1 F:HIS75 3.8 44.3 1.0 CG F:HIS75 4.0 43.9 1.0 N F:THR95 4.0 75.0 1.0 CG G:GLU478 4.1 62.2 1.0 ND1 F:HIS90 4.3 18.5 1.0 CA F:VAL96 4.3 40.7 1.0 CG F:HIS90 4.4 14.3 1.0 O G:THR477 4.5 58.8 1.0 OG1 F:THR95 4.5 45.1 1.0 N F:ASP94 4.7 62.9 1.0 CB G:THR477 4.7 22.1 1.0 CA F:THR95 4.7 72.1 1.0 C F:ASP94 4.7 75.0 1.0 C G:THR477 4.7 36.0 1.0 C F:THR95 4.7 74.6 1.0 CD2 F:PHE71 4.7 30.8 1.0 CA F:ASP94 4.8 64.0 1.0 CA G:GLU478 4.8 22.5 1.0 CG2 F:VAL96 4.8 47.2 1.0 CE2 F:PHE71 4.9 32.2 1.0 N G:GLU478 4.9 29.6 1.0 CB F:THR95 4.9 44.1 1.0 CB G:GLU478 4.9 24.0 1.0 OG1 G:THR477 5.0 37.4 1.0

Zinc binding site 2 out of 2 in the Cation Promoted Association (Cpa) of A Regulatory and Target Protein Is Controlled By Phosphorylation


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Cation Promoted Association (Cpa) of A Regulatory and Target Protein Is Controlled By Phosphorylation within 5.0Å range: probe atom residue distance (Å) B Occ G:Zn502 b:38.6 occ:0.43 O2B G:ADP504 2.9 40.5 1.0 O4P G:G3H503 2.9 75.0 1.0 OD2 G:ASP10 3.1 58.0 1.0 NH1 G:ARG17 3.2 75.0 1.0 OD1 G:ASP10 3.3 38.3 1.0 CG G:ASP10 3.5 47.8 1.0 NH2 G:ARG17 3.6 36.4 1.0 OD2 G:ASP245 3.7 75.0 1.0 O3B G:ADP504 3.8 75.0 1.0 PB G:ADP504 3.9 75.0 1.0 CZ G:ARG17 3.9 75.0 1.0 CG2 G:THR439 4.4 26.2 1.0 P G:G3H503 4.5 75.0 1.0 CG G:ASP245 4.5 53.9 1.0 CB G:ASP245 4.5 17.1 1.0 CB G:THR439 4.6 22.1 1.0 O3A G:ADP504 4.6 75.0 1.0 OG1 G:THR439 4.6 68.3 1.0 O2A G:ADP504 4.6 70.2 1.0 CA G:GLY12 4.7 40.1 1.0 CB G:ASP10 4.8 13.8 1.0 PA G:ADP504 4.9 54.8 1.0 O G:HOH530 4.9 35.9 1.0

M.Feese, D.W.Pettigrew, N.D.Meadow, S.Roseman, S.J.Remington. Cation-Promoted Association of A Regulatory and Target Protein Is Controlled By Protein Phosphorylation. Proc.Natl.Acad.Sci.Usa V. 91 3544 1994.
ISSN: ISSN 0027-8424
PubMed: 8170944
DOI: 10.1073/PNAS.91.9.3544