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Fluorine in PDB 1gvy: Substrate Distorsion By Beta-Mannanase From Pseudomonas Cellulosa

Enzymatic activity of Substrate Distorsion By Beta-Mannanase From Pseudomonas Cellulosa

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

Protein crystallography data

The structure of Substrate Distorsion By Beta-Mannanase From Pseudomonas Cellulosa, PDB code: 1gvy was solved by V.Ducros, D.L.Zechel, H.J.Gilbert, L.Szabo, D.Stoll, 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 / 1.70
Space group P 41
Cell size a, b, c (Å), α, β, γ (°) 93.192, 93.192, 54.343, 90.00, 90.00, 90.00
R / Rfree (%) 14.4 / 17

Other elements in 1gvy:

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

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

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Substrate Distorsion By Beta-Mannanase From Pseudomonas Cellulosa (pdb code 1gvy). 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 Substrate Distorsion By Beta-Mannanase From Pseudomonas Cellulosa, PDB code: 1gvy:

Fluorine binding site 1 out of 1 in 1gvy

Go back to Fluorine Binding Sites List in 1gvy
Fluorine binding site 1 out of 1 in the Substrate Distorsion 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 Distorsion By Beta-Mannanase From Pseudomonas Cellulosa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F1426

b:17.2
occ:1.00
 F2 A:MBF1426 0.0 17.2 1.0
C2 A:MBF1426 1.4 13.8 1.0
C1 A:MBF1426 2.3 15.4 1.0
C3 A:MBF1426 2.4 13.8 1.0
O3 A:MBF1426 2.6 15.2 1.0
O1 A:MBF1426 2.7 17.7 1.0
O A:HOH2262 2.9 15.1 1.0
CE1 A:HIS211 3.0 11.9 1.0
NE2 A:HIS143 3.3 14.2 1.0
O A:HOH2326 3.5 17.9 1.0
OE1 A:GLU320 3.5 16.2 1.0
O5 A:MBF1426 3.6 16.9 1.0
C4 A:MBF1426 3.6 14.0 1.0
NE2 A:HIS211 3.6 10.0 1.0
CE1 A:HIS143 3.7 13.4 1.0
OE2 A:GLU320 3.7 11.1 1.0
C1 A:NIN1422 3.9 17.9 1.0
O22 A:NIN1422 3.9 28.1 1.0
C5 A:MBF1426 4.0 16.3 1.0
ND1 A:HIS211 4.0 10.4 1.0
CD A:GLU320 4.1 13.0 1.0
CZ A:PHE218 4.2 12.8 1.0
CD2 A:HIS143 4.5 15.1 1.0
C6 A:NIN1422 4.6 16.4 1.0
CE1 A:PHE218 4.7 11.6 1.0
ZN A:ZN1425 4.7 12.9 1.0
C2 A:NIN1422 4.7 19.3 1.0
N2 A:NIN1422 4.8 24.9 1.0
O4 A:MBF1426 4.8 14.7 1.0
CZ2 A:TRP360 4.8 14.1 1.0
CH2 A:TRP360 4.9 15.2 1.0
CD2 A:HIS211 4.9 11.6 1.0

Reference:

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
Page generated: Sun Dec 13 11:29:51 2020

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