Chlorine in PDB 8dk9: Sliding-Clamp-Dinx Peptide

Enzymatic activity of Sliding-Clamp-Dinx Peptide

All present enzymatic activity of Sliding-Clamp-Dinx Peptide:
2.7.7.7;

Protein crystallography data

The structure of Sliding-Clamp-Dinx Peptide, PDB code: 8dk9 was solved by M.K.Kapur, O.J.Gray, R.H.Honzatko, S.N.Nelson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.35 / 2.50
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 71.072, 73.944, 81.343, 82.77, 77.57, 87.75
R / Rfree (%) 21.1 / 26.4

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Sliding-Clamp-Dinx Peptide (pdb code 8dk9). 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 Sliding-Clamp-Dinx Peptide, PDB code: 8dk9:

Chlorine binding site 1 out of 1 in 8dk9

Go back to Chlorine Binding Sites List in 8dk9
Chlorine binding site 1 out of 1 in the Sliding-Clamp-Dinx Peptide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Sliding-Clamp-Dinx Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl403

b:43.5
occ:1.00
HH11 C:ARG291 2.4 59.0 1.0
HH11 B:ARG260 2.5 58.9 1.0
H B:ARG260 2.5 50.8 1.0
H B:PHE259 2.5 44.7 1.0
HG3 B:ARG260 2.8 50.6 1.0
HD3 C:ARG291 2.8 55.1 1.0
HA B:LYS258 2.9 51.1 1.0
HD2 B:ARG260 3.1 48.6 1.0
NH1 C:ARG291 3.1 49.1 1.0
N B:PHE259 3.2 37.2 1.0
HB2 B:ARG260 3.3 41.6 1.0
NH1 B:ARG260 3.3 49.1 1.0
N B:ARG260 3.3 42.3 1.0
HH12 C:ARG291 3.5 59.0 1.0
CG B:ARG260 3.5 42.1 1.0
CD1 B:PHE259 3.6 37.6 1.0
HD1 B:PHE259 3.6 45.2 1.0
HH12 B:ARG260 3.6 58.9 1.0
CD C:ARG291 3.7 45.9 1.0
HD2 C:ARG291 3.7 55.1 1.0
CA B:LYS258 3.7 42.6 1.0
CE1 B:PHE259 3.7 38.9 1.0
CB B:ARG260 3.8 34.6 1.0
HB3 B:LYS258 3.8 52.4 1.0
CD B:ARG260 3.8 40.4 1.0
HE1 B:PHE259 3.8 46.7 1.0
C B:LYS258 3.8 45.9 1.0
CG B:PHE259 4.1 32.6 1.0
HG2 B:LYS258 4.1 54.0 1.0
CZ C:ARG291 4.1 39.3 1.0
CA B:PHE259 4.2 41.2 1.0
CA B:ARG260 4.2 42.6 1.0
CB B:LYS258 4.2 43.6 1.0
C B:PHE259 4.2 38.5 1.0
NE C:ARG291 4.3 39.0 1.0
CZ B:PHE259 4.3 29.8 1.0
CZ B:ARG260 4.3 50.7 1.0
HG2 B:ARG260 4.4 50.6 1.0
H B:GLN261 4.5 50.1 1.0
NE B:ARG260 4.5 55.7 1.0
HD3 B:ARG260 4.5 48.6 1.0
O B:PRO257 4.6 39.9 1.0
HB2 C:ARG291 4.6 58.8 1.0
CD2 B:PHE259 4.7 36.2 1.0
HB3 B:ARG260 4.7 41.6 1.0
CG B:LYS258 4.7 45.0 1.0
CB B:PHE259 4.7 40.7 1.0
CE2 B:PHE259 4.8 36.4 1.0
HG3 C:ARG291 4.8 56.5 1.0
HZ B:PHE259 4.8 35.8 1.0
HG3 B:GLN261 4.8 57.8 0.5
CG C:ARG291 4.8 47.1 1.0
HA B:ARG260 4.8 51.1 1.0
O B:LYS258 4.9 50.5 1.0
N B:LYS258 4.9 41.6 1.0

Reference:

M.K.Kapur, O.J.Gray, R.H.Honzatko, S.N.Nelson. Interaction of Sliding Clamp with Mycobacterial Polymerases To Be Published.
Page generated: Tue Jul 30 08:48:25 2024

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