Fluorine in PDB 1gw1: Substrate Distortion By Beta-Mannanase From Pseudomonas Cellulosa

All present enzymatic activity of Substrate Distortion By Beta-Mannanase From Pseudomonas Cellulosa:
3.2.1.78;

The structure of Substrate Distortion By Beta-Mannanase From Pseudomonas Cellulosa, PDB code: 1gw1 was solved by V.Ducros, D.L.Zechel, H.J.Gilbert, L.Szabo, S.G.Withers, G.J.Davies, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.65
Space group	P 41
Cell size a, b, c (Å), α, β, γ (°)	93.488, 93.488, 53.719, 90.00, 90.00, 90.00
R / Rfree (%)	13.8 / 16.7

The structure of Substrate Distortion By Beta-Mannanase From Pseudomonas Cellulosa also contains other interesting chemical elements:

Zinc	(Zn)	2 atoms
Sodium	(Na)	1 atom

The binding sites of Fluorine atom in the Substrate Distortion By Beta-Mannanase From Pseudomonas Cellulosa (pdb code 1gw1). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Substrate Distortion By Beta-Mannanase From Pseudomonas Cellulosa, PDB code: 1gw1:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Substrate Distortion By Beta-Mannanase From Pseudomonas Cellulosa


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Substrate Distortion By Beta-Mannanase From Pseudomonas Cellulosa within 5.0Å range: probe atom residue distance (Å) B Occ A:F1427 b:19.6 occ:0.50 F2 A:MAF1427 0.0 19.6 0.5 C2 A:MAF1427 1.4 17.3 0.5 F2 A:MBF1428 2.0 20.6 0.5 C2 A:MBF1428 2.2 19.9 0.5 C1 A:MAF1427 2.4 18.1 0.5 C3 A:MAF1427 2.4 15.9 0.5 CE1 A:HIS211 2.6 17.4 0.5 O3 A:MAF1427 2.7 15.4 0.5 OE1 A:GLU320 2.7 15.2 0.5 OE1 A:GLU320 2.9 20.4 0.5 NE2 A:HIS211 3.0 17.1 0.5 CE1 A:HIS143 3.0 19.0 1.0 C3 A:MBF1428 3.0 17.8 0.5 OE2 A:GLU320 3.1 19.6 0.5 OE2 A:GLU320 3.1 17.8 0.5 CD A:GLU320 3.2 18.4 0.5 NE2 A:HIS143 3.2 19.1 1.0 CD A:GLU320 3.3 20.4 0.5 CH2 A:TRP360 3.4 15.2 1.0 NE2 A:HIS211 3.5 18.2 0.5 ND1 A:HIS211 3.5 16.8 0.5 C1 A:MBF1428 3.5 20.6 0.5 O5 A:MAF1427 3.6 17.2 0.5 CD2 A:HIS211 3.6 14.3 0.5 CZ2 A:TRP360 3.6 14.0 1.0 O3 A:MBF1428 3.7 16.4 0.5 C4 A:MAF1427 3.8 15.2 0.5 CZ3 A:TRP360 3.8 14.7 1.0 CE1 A:HIS211 3.9 15.9 0.5 ZN A:ZN1424 4.0 15.5 0.5 C5 A:MAF1427 4.1 17.1 0.5 CE2 A:TRP360 4.2 14.5 1.0 O A:HOH2373 4.2 26.4 1.0 ND1 A:HIS143 4.3 18.5 1.0 C4 A:MBF1428 4.4 17.3 0.5 CE3 A:TRP360 4.4 13.9 1.0 O1 A:MBF1428 4.4 23.8 0.5 O5 A:MBF1428 4.5 18.5 0.5 O A:HOH2279 4.5 28.3 1.0 C5 A:MBF1428 4.5 17.8 0.5 CD2 A:HIS143 4.6 17.8 1.0 CG A:GLU320 4.6 22.1 0.5 CD2 A:TRP360 4.6 13.6 1.0 CG A:GLU320 4.6 21.0 0.5 NH2 A:ARG208 4.6 20.8 1.0 O4 A:MAF1427 4.7 14.8 0.5 CD2 A:HIS211 4.7 19.1 0.5 CG A:HIS211 4.7 16.1 0.5 CG A:HIS211 4.7 14.2 0.5 ND1 A:HIS211 4.9 15.2 0.5 O5 A:BMA1426 4.9 14.7 0.5

Fluorine binding site 2 out of 2 in the Substrate Distortion By Beta-Mannanase From Pseudomonas Cellulosa


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Substrate Distortion By Beta-Mannanase From Pseudomonas Cellulosa within 5.0Å range: probe atom residue distance (Å) B Occ A:F1428 b:20.6 occ:0.50 F2 A:MBF1428 0.0 20.6 0.5 O3 A:MAF1427 1.4 15.4 0.5 C2 A:MBF1428 1.4 19.9 0.5 F2 A:MAF1427 2.0 19.6 0.5 C2 A:MAF1427 2.0 17.3 0.5 C3 A:MAF1427 2.0 15.9 0.5 C1 A:MBF1428 2.3 20.6 0.5 C1 A:MAF1427 2.3 18.1 0.5 C3 A:MBF1428 2.4 17.8 0.5 O3 A:MBF1428 2.6 16.4 0.5 O A:HOH2373 2.6 26.4 1.0 O1 A:MBF1428 2.7 23.8 0.5 O5 A:MAF1427 2.8 17.2 0.5 C4 A:MAF1427 3.1 15.2 0.5 NE2 A:HIS211 3.1 17.1 0.5 NE2 A:HIS143 3.2 19.1 1.0 CE1 A:HIS211 3.3 17.4 0.5 C5 A:MAF1427 3.5 17.1 0.5 O5 A:MBF1428 3.6 18.5 0.5 NE2 A:HIS211 3.6 18.2 0.5 O22 A:NIN1429 3.6 32.9 0.5 C4 A:MBF1428 3.6 17.3 0.5 OE2 A:GLU320 3.7 19.6 0.5 O A:HOH2279 3.7 28.3 1.0 OE2 A:GLU320 3.8 17.8 0.5 CE1 A:HIS143 3.8 19.0 1.0 C1 A:NIN1429 3.8 26.6 0.5 OE1 A:GLU320 3.9 20.4 0.5 CZ A:PHE218 3.9 14.8 1.0 CD2 A:HIS211 4.0 14.3 0.5 OE1 A:GLU320 4.0 15.2 0.5 O A:HOH2376 4.0 23.0 0.5 C5 A:MBF1428 4.0 17.8 0.5 CE1 A:HIS211 4.2 15.9 0.5 CD A:GLU320 4.2 20.4 0.5 CD A:GLU320 4.3 18.4 0.5 O4 A:MAF1427 4.3 14.8 0.5 ND1 A:HIS211 4.3 16.8 0.5 CD2 A:HIS143 4.4 17.8 1.0 CE2 A:PHE218 4.5 15.6 1.0 N2 A:NIN1429 4.5 32.4 0.5 C2 A:NIN1429 4.6 29.7 0.5 C6 A:NIN1429 4.6 27.4 0.5 O4 A:MBF1428 4.8 17.1 0.5 CD2 A:HIS211 4.8 19.1 0.5 C6 A:MAF1427 4.8 17.5 0.5 C1 A:BMA1426 4.8 15.4 0.5 O6 A:MAF1427 4.9 19.1 0.5 O5 A:BMA1426 4.9 14.7 0.5 ZN A:ZN1424 5.0 15.5 0.5

V.Ducros, D.L.Zechel, G.Murshudov, H.J.Gilbert, L.Szabo, D.Stoll, S.G.Withers, G.J.Davies. Substrate Distortion By A Beta-Mannanase: Snapshots of the Michaelis and Covalent-Intermediate Complexes Suggest A B2,5 Conformation For the Transition State Angew.Chem.Int.Ed.Engl. V. 41 2824 2002.
ISSN: ISSN 1433-7851
PubMed: 12203498
DOI: 10.1002/1521-3773(20020802)41:15<2824::AID-ANIE2824>3.0.CO;2