Fluorine in PDB 2cit: Structure of the Covalent Intermediate of A Family 26 Lichenase

All present enzymatic activity of Structure of the Covalent Intermediate of A Family 26 Lichenase:
3.2.1.4;

The structure of Structure of the Covalent Intermediate of A Family 26 Lichenase, PDB code: 2cit was solved by V.A.Money, N.L.Smith, A.Scaffidi, R.V.Stick, H.J.Gilbert, G.J.Davies, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.97 / 1.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	49.047, 62.830, 78.057, 90.00, 90.00, 90.00
R / Rfree (%)	15.1 / 17.9

The binding sites of Fluorine atom in the Structure of the Covalent Intermediate of A Family 26 Lichenase (pdb code 2cit). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Structure of the Covalent Intermediate of A Family 26 Lichenase, PDB code: 2cit:

Fluorine binding site 1 out of 1 in the Structure of the Covalent Intermediate of A Family 26 Lichenase


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Structure of the Covalent Intermediate of A Family 26 Lichenase within 5.0Å range: probe atom residue distance (Å) B Occ A:F1283 b:4.8 occ:1.00 F2 A:G2F1283 0.0 4.8 1.0 C2 A:G2F1283 1.4 3.8 1.0 C1 A:G2F1283 2.4 5.6 1.0 C3 A:G2F1283 2.4 4.2 1.0 OE1 A:GLU222 2.7 5.4 1.0 OE2 A:GLU222 2.8 5.5 1.0 O3 A:G2F1283 2.9 3.0 1.0 OH A:TYR115 3.0 3.5 1.0 CD A:GLU222 3.0 6.0 1.0 C1 A:BGC1284 3.0 3.8 1.0 NE2 A:HIS108 3.2 4.9 1.0 CE1 A:PHE41 3.3 3.6 1.0 O5 A:G2F1283 3.6 6.8 1.0 C4 A:G2F1283 3.7 5.8 1.0 CZ A:PHE41 3.7 2.7 1.0 O2 A:BGC1284 3.8 3.8 1.0 CE1 A:HIS108 3.9 3.2 1.0 C5 A:G2F1283 4.0 7.0 1.0 O A:HOH2245 4.0 10.4 1.0 C2 A:BGC1284 4.1 2.9 1.0 O5 A:BGC1284 4.1 2.8 1.0 CD2 A:HIS108 4.2 3.1 1.0 CZ A:TYR115 4.3 2.4 1.0 CD1 A:PHE41 4.3 2.5 1.0 CG A:GLU222 4.4 9.1 1.0 OE2 A:GLU70 4.4 5.1 1.0 O A:HOH2248 4.8 24.9 1.0 O4 A:G2F1283 4.8 4.8 1.0 CE2 A:TYR115 4.8 2.9 1.0 NH2 A:ARG105 4.9 3.3 1.0 C5 A:BGC1284 4.9 2.4 1.0 CE2 A:PHE41 4.9 4.2 1.0 C3 A:BGC1284 4.9 2.8 1.0 CE1 A:PHE256 5.0 3.4 1.0 O A:HOH2483 5.0 16.1 1.0

V.A.Money, N.L.Smith, A.Scaffidi, R.V.Stick, H.J.Gilbert, G.J.Davies. Substrate Distortion By A Lichenase Highlights the Different Conformational Itineraries Harnessed By Related Glycoside Hydrolases. Angew.Chem.Int.Ed.Engl. V. 45 5136 2006.
ISSN: ISSN 1433-7851
PubMed: 16823793
DOI: 10.1002/ANIE.200600802