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Chlorine in PDB 5luj: Structure of Cutinase 2 From Thermobifida Cellulosilytica

Protein crystallography data

The structure of Structure of Cutinase 2 From Thermobifida Cellulosilytica, PDB code: 5luj was solved by A.Hromic, A.Lyskowski, K.Gruber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.52 / 2.20
Space group P 2 21 21
Cell size a, b, c (Å), α, β, γ (°) 36.670, 43.150, 152.350, 90.00, 90.00, 90.00
R / Rfree (%) 18.3 / 24.1

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of Cutinase 2 From Thermobifida Cellulosilytica (pdb code 5luj). 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 Cutinase 2 From Thermobifida Cellulosilytica, PDB code: 5luj:

Chlorine binding site 1 out of 1 in 5luj

Go back to Chlorine Binding Sites List in 5luj
Chlorine binding site 1 out of 1 in the Structure of Cutinase 2 From Thermobifida Cellulosilytica


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Cutinase 2 From Thermobifida Cellulosilytica within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl301

b:8.7
occ:0.50
N A:ARG29 3.1 3.8 1.0
NH1 A:ARG29 3.3 11.4 1.0
CG A:ARG29 3.6 13.0 1.0
CA A:GLU28 3.7 9.9 1.0
CD A:ARG29 3.9 18.4 1.0
CB A:ARG29 3.9 6.3 1.0
C A:GLU28 3.9 8.6 1.0
CA A:ARG29 4.0 7.3 1.0
CZ A:ARG29 4.1 20.8 1.0
CG A:GLU28 4.2 8.7 1.0
NE A:ARG29 4.3 22.1 1.0
CB A:GLU28 4.3 5.0 1.0
O A:GLU27 4.5 8.4 1.0
O A:ARG29 4.5 7.2 1.0
O A:HOH410 4.7 5.2 1.0
C A:ARG29 4.8 10.6 1.0
N A:GLU28 4.8 4.1 1.0

Reference:

D.Ribitsch, A.Hromic, S.Zitzenbacher, B.Zartl, C.Gamerith, A.Pellis, A.Jungbauer, A.Yskowski, G.Steinkellner, K.Gruber, R.Tscheliessnig, E.Herrero Acero, G.M.Guebitz. Small Cause, Large Effect: Structural Characterization of Cutinases From Thermobifida Cellulosilytica. Biotechnol. Bioeng. V. 114 2481 2017.
ISSN: ESSN 1097-0290
PubMed: 28671263
DOI: 10.1002/BIT.26372
Page generated: Sat Jul 12 05:08:52 2025

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