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Chlorine in PDB 6kg0: Nifs From Helicobacter Pylori, Soaked with L-Cysteine For 118 Sec

Enzymatic activity of Nifs From Helicobacter Pylori, Soaked with L-Cysteine For 118 Sec

All present enzymatic activity of Nifs From Helicobacter Pylori, Soaked with L-Cysteine For 118 Sec:
2.8.1.7;

Protein crystallography data

The structure of Nifs From Helicobacter Pylori, Soaked with L-Cysteine For 118 Sec, PDB code: 6kg0 was solved by R.Nakamura, Y.Takahashi, T.Fujishiro, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.20 / 2.78
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 103.200, 103.200, 134.100, 90.00, 90.00, 90.00
R / Rfree (%) 18.4 / 22.1

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Nifs From Helicobacter Pylori, Soaked with L-Cysteine For 118 Sec (pdb code 6kg0). 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 Nifs From Helicobacter Pylori, Soaked with L-Cysteine For 118 Sec, PDB code: 6kg0:

Chlorine binding site 1 out of 1 in 6kg0

Go back to Chlorine Binding Sites List in 6kg0
Chlorine binding site 1 out of 1 in the Nifs From Helicobacter Pylori, Soaked with L-Cysteine For 118 Sec


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Nifs From Helicobacter Pylori, Soaked with L-Cysteine For 118 Sec within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl502

b:79.1
occ:1.00
O A:PRO226 3.3 73.5 1.0
CD1 A:LEU227 3.8 56.2 1.0
CA A:LEU227 4.1 60.2 1.0
C A:PRO226 4.3 67.9 1.0
CE2 A:PHE86 4.4 85.8 1.0
O A:LYS82 4.5 82.4 1.0
CG2 A:THR225 4.5 77.1 1.0
CD2 A:PHE86 4.5 84.5 1.0
N A:LEU227 4.6 61.5 1.0
CB A:LYS82 4.7 65.8 1.0
O A:THR225 4.7 83.5 1.0
CB A:LEU227 4.8 58.7 1.0
C A:LYS82 4.9 76.9 1.0
CE1 A:HIS229 4.9 80.9 1.0
CG A:LEU227 4.9 55.5 1.0
O A:LEU227 4.9 59.7 1.0

Reference:

R.Nakamura, M.Hikita, S.Ogawa, Y.Takahashi, T.Fujishiro. Snapshots of Plp-Substrate and Plp-Product External Aldimines As Intermediates in Two Types of Cysteine Desulfurase Enzymes. Febs J. 2019.
ISSN: ISSN 1742-464X
PubMed: 31587510
DOI: 10.1111/FEBS.15081
Page generated: Sun Jul 28 02:28:03 2024

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