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Chlorine in PDB 3v16: An Intramolecular Pi-Cation Latch in Phosphatidylinositol-Specific Phospholipase C From S.Aureus Controls Substrate Access to the Active Site

Enzymatic activity of An Intramolecular Pi-Cation Latch in Phosphatidylinositol-Specific Phospholipase C From S.Aureus Controls Substrate Access to the Active Site

All present enzymatic activity of An Intramolecular Pi-Cation Latch in Phosphatidylinositol-Specific Phospholipase C From S.Aureus Controls Substrate Access to the Active Site:
4.6.1.13;

Protein crystallography data

The structure of An Intramolecular Pi-Cation Latch in Phosphatidylinositol-Specific Phospholipase C From S.Aureus Controls Substrate Access to the Active Site, PDB code: 3v16 was solved by R.I.Goldstein, J.Cheng, B.Stec, M.F.Roberts, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.94 / 2.05
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 104.161, 43.607, 62.218, 90.00, 90.00, 90.00
R / Rfree (%) 15.6 / 21.3

Chlorine Binding Sites:

The binding sites of Chlorine atom in the An Intramolecular Pi-Cation Latch in Phosphatidylinositol-Specific Phospholipase C From S.Aureus Controls Substrate Access to the Active Site (pdb code 3v16). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the An Intramolecular Pi-Cation Latch in Phosphatidylinositol-Specific Phospholipase C From S.Aureus Controls Substrate Access to the Active Site, PDB code: 3v16:

Chlorine binding site 1 out of 1 in 3v16

Go back to Chlorine Binding Sites List in 3v16
Chlorine binding site 1 out of 1 in the An Intramolecular Pi-Cation Latch in Phosphatidylinositol-Specific Phospholipase C From S.Aureus Controls Substrate Access to the Active Site


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of An Intramolecular Pi-Cation Latch in Phosphatidylinositol-Specific Phospholipase C From S.Aureus Controls Substrate Access to the Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl402

b:34.9
occ:1.00
 N A:LYS38 3.2 28.1 1.0
NE2 A:HIS86 3.3 31.4 1.0
N A:ASP39 3.4 26.8 1.0
CB A:ASP39 3.6 25.6 1.0
CD2 A:LEU37 3.8 29.1 1.0
CA A:LEU37 3.8 27.8 1.0
C A:LEU37 4.0 28.3 1.0
CE1 A:HIS86 4.1 32.3 1.0
CA A:LYS38 4.1 28.5 1.0
CA A:ASP39 4.2 25.9 1.0
NZ A:LYS42 4.2 43.3 1.0
C A:LYS38 4.2 27.5 1.0
CB A:LEU37 4.4 28.0 1.0
CD2 A:HIS86 4.4 30.7 1.0
O A:THR36 4.4 26.1 1.0
CB A:LYS38 4.4 28.8 1.0
CD A:LYS42 4.5 36.9 1.0
CG A:LEU37 4.7 28.5 1.0
N A:LEU37 4.9 27.3 1.0
CE A:LYS42 4.9 39.7 1.0
CG A:ASP39 5.0 27.1 1.0

Reference:

R.Goldstein, J.Cheng, B.Stec, M.F.Roberts. Structure of the S. Aureus Pi-Specific Phospholipase C Reveals Modulation of Active Site Access By A Titratable Pi-Cation Latched Loop Biochemistry V. 51 2579 2012.
ISSN: ISSN 0006-2960
PubMed: 22390775
DOI: 10.1021/BI300057Q
Page generated: Fri Jul 11 11:33:33 2025

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