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Fluorine in PDB 1h4g: Oligosaccharide-Binding to Family 11 Xylanases: Both Covalent Intermediate and Mutant-Product Complexes Display 2,5B Conformations at the Active-Centre

Enzymatic activity of Oligosaccharide-Binding to Family 11 Xylanases: Both Covalent Intermediate and Mutant-Product Complexes Display 2,5B Conformations at the Active-Centre

All present enzymatic activity of Oligosaccharide-Binding to Family 11 Xylanases: Both Covalent Intermediate and Mutant-Product Complexes Display 2,5B Conformations at the Active-Centre:
3.2.1.8;

Protein crystallography data

The structure of Oligosaccharide-Binding to Family 11 Xylanases: Both Covalent Intermediate and Mutant-Product Complexes Display 2,5B Conformations at the Active-Centre, PDB code: 1h4g was solved by E.Sabini, K.S.Wilson, S.Danielsen, M.Schulein, G.J.Davies, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 72.061, 75.098, 78.270, 90.00, 90.00, 90.00
R / Rfree (%) 15.8 / 18.1

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Oligosaccharide-Binding to Family 11 Xylanases: Both Covalent Intermediate and Mutant-Product Complexes Display 2,5B Conformations at the Active-Centre (pdb code 1h4g). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Oligosaccharide-Binding to Family 11 Xylanases: Both Covalent Intermediate and Mutant-Product Complexes Display 2,5B Conformations at the Active-Centre, PDB code: 1h4g:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in 1h4g

Go back to Fluorine Binding Sites List in 1h4g
Fluorine binding site 1 out of 2 in the Oligosaccharide-Binding to Family 11 Xylanases: Both Covalent Intermediate and Mutant-Product Complexes Display 2,5B Conformations at the Active-Centre


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Oligosaccharide-Binding to Family 11 Xylanases: Both Covalent Intermediate and Mutant-Product Complexes Display 2,5B Conformations at the Active-Centre within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F1207

b:10.4
occ:1.00
F2A A:FXP1207 0.0 10.4 1.0
C2A A:FXP1207 1.4 9.7 1.0
C3A A:FXP1207 2.4 9.3 1.0
C1A A:FXP1207 2.4 9.2 1.0
OE1 A:GLU94 2.8 9.3 1.0
OE2 A:GLU94 2.8 8.8 1.0
O3A A:FXP1207 2.8 10.9 1.0
NE A:ARG129 3.0 11.9 1.0
CD A:GLU94 3.1 8.6 1.0
NE2 A:GLN143 3.3 9.6 1.0
CZ A:PHE141 3.4 11.1 1.0
CE2 A:PHE141 3.4 10.1 1.0
O5A A:FXP1207 3.6 9.4 1.0
CG A:ARG129 3.6 10.7 1.0
CD A:ARG129 3.7 11.8 1.0
CZ A:ARG129 3.7 11.3 1.0
C4A A:FXP1207 3.7 9.7 1.0
NH2 A:ARG129 3.7 11.5 1.0
O A:HOH2226 3.8 22.1 1.0
C5A A:FXP1207 4.0 9.8 1.0
O A:HOH2110 4.1 13.0 1.0
CD A:GLN143 4.2 8.6 1.0
CG A:GLU94 4.4 8.7 1.0
O4A A:FXP1207 4.5 9.8 1.0
CG A:GLN143 4.5 8.8 1.0
CB A:ARG129 4.6 10.2 1.0
O A:PRO133 4.7 11.2 1.0
CB A:GLU94 4.7 8.8 1.0
CD2 A:PHE141 4.8 10.9 1.0
CE1 A:PHE141 4.8 11.1 1.0
O A:HOH2173 4.8 19.2 1.0
OH A:TYR96 4.9 9.7 1.0
CH2 A:TRP87 4.9 9.5 1.0
NH1 A:ARG129 4.9 13.6 1.0

Fluorine binding site 2 out of 2 in 1h4g

Go back to Fluorine Binding Sites List in 1h4g
Fluorine binding site 2 out of 2 in the Oligosaccharide-Binding to Family 11 Xylanases: Both Covalent Intermediate and Mutant-Product Complexes Display 2,5B Conformations at the Active-Centre


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Oligosaccharide-Binding to Family 11 Xylanases: Both Covalent Intermediate and Mutant-Product Complexes Display 2,5B Conformations at the Active-Centre within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F1208

b:11.3
occ:1.00
F2A B:FXP1208 0.0 11.3 1.0
C2A B:FXP1208 1.4 10.0 1.0
C1A B:FXP1208 2.4 10.0 1.0
C3A B:FXP1208 2.4 10.0 1.0
O3A B:FXP1208 2.8 11.5 1.0
OE2 B:GLU94 2.8 9.7 1.0
OE1 B:GLU94 2.8 10.4 1.0
NE B:ARG129 2.9 22.0 1.0
CD B:GLU94 3.1 10.1 1.0
CZ B:PHE141 3.2 12.2 1.0
CE2 B:PHE141 3.2 12.1 1.0
NE2 B:GLN143 3.5 12.1 1.0
NH2 B:ARG129 3.5 21.4 1.0
CZ B:ARG129 3.6 23.5 1.0
O5A B:FXP1208 3.6 10.1 1.0
C4A B:FXP1208 3.7 9.8 1.0
CG B:ARG129 3.8 15.2 1.0
CD B:ARG129 3.8 19.4 1.0
O B:HOH2195 3.8 43.6 1.0
C5A B:FXP1208 4.0 10.4 1.0
O B:HOH2257 4.0 17.7 1.0
O B:HOH2154 4.4 25.5 1.0
CD B:GLN143 4.4 11.7 1.0
CG B:GLU94 4.5 9.6 1.0
O4A B:FXP1208 4.5 9.9 1.0
CE1 B:PHE141 4.6 12.3 1.0
CD2 B:PHE141 4.6 11.9 1.0
CB B:ARG129 4.7 13.4 1.0
O B:PRO133 4.7 12.0 1.0
CG B:GLN143 4.8 12.6 1.0
NH1 B:ARG129 4.8 26.4 1.0
CB B:GLU94 4.8 9.4 1.0
OH B:TYR96 5.0 10.4 1.0

Reference:

E.Sabini, G.Sulzenbacher, M.Dauter, Z.Dauter, P.L.Jorgensen, M.Schulein, C.Dupont, G.J.Davies, K.S.Wilson. Catalysis and Specificity in Enzymatic Glycoside Hydrolysis: A 2,5B Conformation For the Glycosyl-Enzyme Intermediate Revealed By the Structure of the Bacillus Agaradhaerens Family 11 Xylanase. Chem.Biol. V. 6 483 1999.
ISSN: ISSN 1074-5521
PubMed: 10381409
DOI: 10.1016/S1074-5521(99)80066-0
Page generated: Wed Jul 31 11:30:37 2024

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