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Chlorine in PDB 5ktp: Crystal Structure of Pyrococcus Horikoshii Quinolinate Synthase (Nada) with Bound Itaconate and FE4S4 Cluster

Enzymatic activity of Crystal Structure of Pyrococcus Horikoshii Quinolinate Synthase (Nada) with Bound Itaconate and FE4S4 Cluster

All present enzymatic activity of Crystal Structure of Pyrococcus Horikoshii Quinolinate Synthase (Nada) with Bound Itaconate and FE4S4 Cluster:
2.5.1.72;

Protein crystallography data

The structure of Crystal Structure of Pyrococcus Horikoshii Quinolinate Synthase (Nada) with Bound Itaconate and FE4S4 Cluster, PDB code: 5ktp was solved by M.K.Fenwick, S.E.Ealick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.63 / 1.54
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 47.477, 52.671, 55.686, 90.00, 112.41, 90.00
R / Rfree (%) 15.5 / 19.8

Other elements in 5ktp:

The structure of Crystal Structure of Pyrococcus Horikoshii Quinolinate Synthase (Nada) with Bound Itaconate and FE4S4 Cluster also contains other interesting chemical elements:

Iron (Fe) 4 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Pyrococcus Horikoshii Quinolinate Synthase (Nada) with Bound Itaconate and FE4S4 Cluster (pdb code 5ktp). 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 Crystal Structure of Pyrococcus Horikoshii Quinolinate Synthase (Nada) with Bound Itaconate and FE4S4 Cluster, PDB code: 5ktp:

Chlorine binding site 1 out of 1 in 5ktp

Go back to Chlorine Binding Sites List in 5ktp
Chlorine binding site 1 out of 1 in the Crystal Structure of Pyrococcus Horikoshii Quinolinate Synthase (Nada) with Bound Itaconate and FE4S4 Cluster


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Pyrococcus Horikoshii Quinolinate Synthase (Nada) with Bound Itaconate and FE4S4 Cluster within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl402

b:20.0
occ:1.00
NE2 A:GLN244 3.3 21.6 1.0
CD1 A:TYR242 3.9 10.5 1.0
CE1 A:TYR242 4.1 9.8 1.0
CD A:GLN244 4.3 18.0 1.0
OE1 A:GLN244 4.4 17.9 1.0

Reference:

M.K.Fenwick, S.E.Ealick. Crystal Structures of the Iron-Sulfur Cluster-Dependent Quinolinate Synthase in Complex with Dihydroxyacetone Phosphate, Iminoaspartate Analogues, and Quinolinate. Biochemistry V. 55 4135 2016.
ISSN: ISSN 0006-2960
PubMed: 27404889
DOI: 10.1021/ACS.BIOCHEM.6B00626
Page generated: Sat Dec 12 11:57:38 2020

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