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Chlorine in PDB 5llf: Structure of Polyphosphate Kinase 2 Mutant D117N From Francisella Tularensis with Polyphosphate

Enzymatic activity of Structure of Polyphosphate Kinase 2 Mutant D117N From Francisella Tularensis with Polyphosphate

All present enzymatic activity of Structure of Polyphosphate Kinase 2 Mutant D117N From Francisella Tularensis with Polyphosphate:
2.7.4.1;

Protein crystallography data

The structure of Structure of Polyphosphate Kinase 2 Mutant D117N From Francisella Tularensis with Polyphosphate, PDB code: 5llf was solved by P.L.Roach, A.E.Parnell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 69.50 / 2.31
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 73.440, 165.940, 255.300, 90.00, 90.00, 90.00
R / Rfree (%) 19.8 / 24.7

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of Polyphosphate Kinase 2 Mutant D117N From Francisella Tularensis with Polyphosphate (pdb code 5llf). 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 Structure of Polyphosphate Kinase 2 Mutant D117N From Francisella Tularensis with Polyphosphate, PDB code: 5llf:

Chlorine binding site 1 out of 1 in 5llf

Go back to Chlorine Binding Sites List in 5llf
Chlorine binding site 1 out of 1 in the Structure of Polyphosphate Kinase 2 Mutant D117N From Francisella Tularensis with Polyphosphate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Polyphosphate Kinase 2 Mutant D117N From Francisella Tularensis with Polyphosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl302

b:69.5
occ:1.00
NH2 C:ARG9 3.8 57.2 1.0
NH1 C:ARG9 3.8 59.7 1.0
OG1 C:THR263 3.9 57.3 1.0
N C:THR263 4.0 53.5 1.0
CD C:LYS266 4.2 75.3 1.0
CG2 C:THR263 4.3 51.6 1.0
CA C:GLY262 4.3 50.4 1.0
CZ C:ARG9 4.3 63.5 1.0
CB C:THR263 4.6 54.4 1.0
C C:GLY262 4.6 51.7 1.0
CE C:LYS266 4.7 79.5 1.0
CG C:LYS266 4.7 61.5 1.0
O C:VAL261 4.8 50.5 1.0
CA C:THR263 4.9 54.5 1.0

Reference:

A.E.Parnell, S.Mordhorst, F.Kemper, M.Giurrandino, J.P.Prince, N.J.Schwarzer, A.Hofer, D.Wohlwend, H.J.Jessen, S.Gerhardt, O.Einsle, P.C.F.Oyston, J.N.Andexer, P.L.Roach. Substrate Recognition and Mechanism Revealed By Ligand-Bound Polyphosphate Kinase 2 Structures. Proc. Natl. Acad. Sci. V. 115 3350 2018U.S.A..
ISSN: ESSN 1091-6490
PubMed: 29531036
DOI: 10.1073/PNAS.1710741115
Page generated: Sat Dec 12 12:03:26 2020

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