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Chlorine in PDB 5oe0: Crystal Structure of the Beta-Lactamase Oxa-181

Enzymatic activity of Crystal Structure of the Beta-Lactamase Oxa-181

All present enzymatic activity of Crystal Structure of the Beta-Lactamase Oxa-181:
3.5.2.6;

Protein crystallography data

The structure of Crystal Structure of the Beta-Lactamase Oxa-181, PDB code: 5oe0 was solved by B.A.Lund, T.J.O.Carlsen, H.K.S.Leiros, A.M.Thomassen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.98 / 2.05
Space group P 62
Cell size a, b, c (Å), α, β, γ (°) 143.927, 143.927, 53.542, 90.00, 90.00, 120.00
R / Rfree (%) 20.2 / 24.2

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the Beta-Lactamase Oxa-181 (pdb code 5oe0). 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 the Beta-Lactamase Oxa-181, PDB code: 5oe0:

Chlorine binding site 1 out of 1 in 5oe0

Go back to Chlorine Binding Sites List in 5oe0
Chlorine binding site 1 out of 1 in the Crystal Structure of the Beta-Lactamase Oxa-181


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 the Beta-Lactamase Oxa-181 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl301

b:27.0
occ:1.00
HH22 B:ARG206 2.3 30.4 1.0
HH22 A:ARG206 2.3 31.1 1.0
HH12 A:ARG206 2.4 32.4 1.0
HH12 B:ARG206 2.5 29.1 1.0
NH2 B:ARG206 3.0 25.4 1.0
NH2 A:ARG206 3.1 25.9 1.0
NH1 A:ARG206 3.2 27.0 1.0
HD22 A:LEU196 3.2 23.8 1.0
NH1 B:ARG206 3.2 24.2 1.0
HD22 B:LEU196 3.3 25.8 1.0
HA B:GLN193 3.4 27.4 1.0
HA A:GLN193 3.4 31.0 1.0
CZ A:ARG206 3.5 24.6 1.0
CZ B:ARG206 3.6 22.1 1.0
HG3 B:GLN193 3.6 27.2 1.0
HG3 A:GLN193 3.7 28.6 1.0
HH21 B:ARG206 3.7 30.4 1.0
HH21 A:ARG206 3.7 31.1 1.0
HH11 A:ARG206 3.9 32.4 1.0
HH11 B:ARG206 4.0 29.1 1.0
HB2 A:LEU196 4.1 23.4 1.0
HB2 B:LEU196 4.1 23.0 1.0
HB2 B:GLN193 4.1 24.2 1.0
HB2 A:GLN193 4.1 28.5 1.0
CD2 A:LEU196 4.2 19.9 1.0
CD2 B:LEU196 4.3 21.5 1.0
CA B:GLN193 4.3 22.8 1.0
CA A:GLN193 4.3 25.8 1.0
HD13 A:LEU196 4.4 26.6 1.0
CG B:GLN193 4.5 22.6 1.0
CB B:GLN193 4.5 20.1 1.0
CG A:GLN193 4.5 23.9 1.0
HD23 A:LEU196 4.5 23.8 1.0
CB A:GLN193 4.5 23.7 1.0
HD13 B:LEU196 4.5 27.0 1.0
HD23 B:LEU196 4.6 25.8 1.0
HD21 A:LEU196 4.6 23.8 1.0
HD21 B:LEU196 4.7 25.8 1.0
NE A:ARG206 4.8 23.9 1.0
CB A:LEU196 4.9 19.5 1.0
O B:HOH344 4.9 38.5 1.0
NE B:ARG206 4.9 23.0 1.0
CB B:LEU196 4.9 19.2 1.0
CG A:LEU196 5.0 18.6 1.0

Reference:

B.A.Lund, A.M.Thomassen, T.J.O.Carlsen, H.K.S.Leiros. Structure, Activity and Thermostability Investigations of Oxa-163, Oxa-181 and Oxa-245 Using Biochemical Analysis, Crystal Structures and Differential Scanning Calorimetry Analysis. Acta Crystallogr F Struct V. 73 579 2017BIOL Commun.
ISSN: ESSN 2053-230X
PubMed: 28994407
DOI: 10.1107/S2053230X17013838
Page generated: Fri Jul 26 14:25:38 2024

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