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Chlorine in PDB 3pig: Beta-Fructofuranosidase From Bifidobacterium Longum

Enzymatic activity of Beta-Fructofuranosidase From Bifidobacterium Longum

All present enzymatic activity of Beta-Fructofuranosidase From Bifidobacterium Longum:
3.2.1.26;

Protein crystallography data

The structure of Beta-Fructofuranosidase From Bifidobacterium Longum, PDB code: 3pig was solved by A.Bujacz, G.Bujacz, I.Redzynia, M.Krzepkowska-Jedrzejczak, S.Bielecki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 75.45 / 1.87
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 87.117, 87.117, 223.942, 90.00, 90.00, 120.00
R / Rfree (%) 14.9 / 19.9

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Beta-Fructofuranosidase From Bifidobacterium Longum (pdb code 3pig). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 6 binding sites of Chlorine where determined in the Beta-Fructofuranosidase From Bifidobacterium Longum, PDB code: 3pig:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6;

Chlorine binding site 1 out of 6 in 3pig

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Chlorine binding site 1 out of 6 in the Beta-Fructofuranosidase From Bifidobacterium Longum


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Beta-Fructofuranosidase From Bifidobacterium Longum within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl527

b:27.6
occ:1.00
 N A:GLU387 3.2 21.9 1.0
N A:ALA388 3.3 17.0 1.0
O A:HOH1024 3.4 15.9 1.0
ND1 A:HIS511 3.5 25.0 1.0
O A:ALA388 3.7 18.7 1.0
CB A:GLU387 3.7 23.4 1.0
CA A:GLU387 3.8 21.6 1.0
O A:HOH1016 3.9 35.9 1.0
CG1 A:VAL389 3.9 15.8 1.0
C A:GLU387 4.1 20.2 1.0
CE1 A:HIS511 4.1 23.5 1.0
C A:ALA388 4.2 17.0 1.0
C A:ALA386 4.2 22.4 1.0
CA A:ALA386 4.2 22.7 1.0
CA A:ALA388 4.3 17.1 1.0
O A:ASP385 4.3 28.8 1.0
O A:HOH580 4.4 24.2 1.0
OE1 A:GLU387 4.6 34.7 1.0
CG A:HIS511 4.7 22.9 1.0
CG A:GLU387 4.7 26.8 1.0
CB A:ALA388 4.8 17.2 1.0

Chlorine binding site 2 out of 6 in 3pig

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Chlorine binding site 2 out of 6 in the Beta-Fructofuranosidase From Bifidobacterium Longum


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Beta-Fructofuranosidase From Bifidobacterium Longum within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl528

b:31.0
occ:1.00
 O A:HOH1177 3.1 22.7 1.0
O A:HOH654 3.1 13.8 1.0
NH1 A:ARG428 3.2 16.0 1.0
NH2 A:ARG428 3.2 17.5 1.0
O A:HOH797 3.3 17.5 1.0
CZ A:ARG428 3.7 19.1 1.0
CB A:MET266 3.9 19.9 1.0
CE A:MET266 3.9 20.8 1.0
N A:MET266 4.0 18.3 1.0
CB A:PHE265 4.1 17.1 1.0
C A:PHE265 4.1 16.6 1.0
CA A:MET266 4.2 18.2 1.0
O A:HOH628 4.2 14.5 1.0
O A:PHE265 4.5 18.1 1.0
CA A:PHE265 4.6 17.7 1.0
O A:HOH919 4.7 14.1 1.0
N A:PHE265 4.8 17.3 1.0
CG A:MET266 4.8 21.1 1.0
SD A:MET266 4.9 26.0 1.0
NE A:ARG428 5.0 17.6 1.0

Chlorine binding site 3 out of 6 in 3pig

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Chlorine binding site 3 out of 6 in the Beta-Fructofuranosidase From Bifidobacterium Longum


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Beta-Fructofuranosidase From Bifidobacterium Longum within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl529

b:36.3
occ:1.00
 O A:HOH863 2.6 19.9 1.0
O A:HOH1069 2.7 13.6 1.0
O A:ALA486 2.9 17.6 1.0
C A:SER487 3.4 18.6 1.0
O A:SER487 3.4 18.7 1.0
N A:GLU488 3.7 19.4 1.0
NE1 A:TRP39 3.8 17.6 1.0
C A:ALA486 3.9 16.9 1.0
CA A:GLU488 3.9 19.3 1.0
CA A:SER487 4.0 18.0 1.0
CD A:ARG38 4.1 19.2 1.0
NH2 A:ARG491 4.1 15.8 1.0
CG A:GLU488 4.2 24.8 1.0
CB A:ARG38 4.2 17.9 1.0
CE2 A:TRP39 4.3 16.0 1.0
CZ2 A:TRP39 4.3 19.9 1.0
O A:HOH601 4.3 13.1 1.0
N A:SER487 4.4 16.1 1.0
CD A:GLU488 4.4 32.1 1.0
OE2 A:GLU488 4.5 36.8 1.0
CG A:ARG38 4.5 16.9 1.0
CB A:GLU488 4.7 20.9 1.0
O A:HOH806 4.7 34.8 1.0
CD1 A:TRP39 4.7 17.9 1.0
O A:HOH721 4.9 16.8 1.0
OE1 A:GLU488 5.0 28.1 1.0

Chlorine binding site 4 out of 6 in 3pig

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Chlorine binding site 4 out of 6 in the Beta-Fructofuranosidase From Bifidobacterium Longum


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Beta-Fructofuranosidase From Bifidobacterium Longum within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl527

b:31.9
occ:1.00
 O B:HOH873 3.0 24.2 1.0
NH2 B:ARG428 3.1 17.9 1.0
O B:HOH677 3.1 15.9 1.0
O B:HOH653 3.2 13.0 1.0
NH1 B:ARG428 3.2 17.6 1.0
O B:HOH991 3.5 36.6 1.0
CZ B:ARG428 3.6 21.1 1.0
CB B:MET266 3.9 21.4 1.0
CB B:PHE265 4.0 17.9 1.0
N B:MET266 4.1 19.4 1.0
C B:PHE265 4.2 18.6 1.0
CE B:MET266 4.2 25.9 1.0
CA B:MET266 4.3 20.3 1.0
O B:HOH557 4.4 11.4 1.0
O B:PHE265 4.5 19.2 1.0
CA B:PHE265 4.5 18.1 1.0
O B:HOH713 4.5 15.2 1.0
N B:PHE265 4.8 18.4 1.0
CG B:MET266 4.9 24.5 1.0
NE B:ARG428 4.9 20.2 1.0
SD B:MET266 5.0 27.4 1.0

Chlorine binding site 5 out of 6 in 3pig

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Chlorine binding site 5 out of 6 in the Beta-Fructofuranosidase From Bifidobacterium Longum


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Beta-Fructofuranosidase From Bifidobacterium Longum within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl528

b:28.0
occ:1.00
 N B:GLU387 3.2 18.7 1.0
N B:ALA388 3.3 19.3 1.0
O B:HOH913 3.5 34.4 1.0
O B:HOH778 3.6 15.5 1.0
CB B:GLU387 3.6 22.6 1.0
CD2 B:HIS511 3.7 20.2 1.0
O B:ALA388 3.7 20.0 1.0
CA B:GLU387 3.8 21.2 1.0
CG1 B:VAL389 3.9 16.8 1.0
C B:GLU387 4.1 20.2 1.0
C B:ALA386 4.2 20.5 1.0
O B:HOH652 4.2 16.4 1.0
CA B:ALA386 4.2 20.4 1.0
C B:ALA388 4.2 19.0 1.0
CA B:ALA388 4.3 19.2 1.0
O B:ASP385 4.3 22.9 1.0
NE2 B:HIS511 4.5 19.3 1.0
O B:HOH802 4.6 23.4 1.0
CG B:HIS511 4.7 21.6 1.0
CB B:ALA388 4.9 17.7 1.0
CG B:GLU387 4.9 29.9 1.0

Chlorine binding site 6 out of 6 in 3pig

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Chlorine binding site 6 out of 6 in the Beta-Fructofuranosidase From Bifidobacterium Longum


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of Beta-Fructofuranosidase From Bifidobacterium Longum within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl529

b:29.7
occ:1.00
 O B:HOH652 3.0 16.4 1.0
OD1 B:ASP384 3.1 21.8 0.5
N B:ASP384 3.2 21.0 1.0
N B:ASP385 3.3 21.9 1.0
CB B:ALA383 3.6 20.6 1.0
CA B:ALA383 3.8 20.4 1.0
C B:ALA383 3.9 20.8 1.0
O B:ASP385 3.9 22.9 1.0
C B:ASP385 4.0 22.2 1.0
CA B:ASP384 4.0 22.7 0.5
CA B:ASP384 4.1 22.4 0.5
CA B:ASP385 4.1 22.3 1.0
C B:ASP384 4.1 22.6 1.0
CG B:ASP384 4.2 23.8 0.5
CB B:ASP384 4.4 23.5 0.5
O B:HOH1068 4.5 31.0 1.0
N B:ALA386 4.6 21.4 1.0
CB B:ASP384 4.6 23.2 0.5
CB B:ASP385 4.6 24.6 1.0

Reference:

A.Bujacz, M.Jedrzejczak-Krzepkowska, S.Bielecki, I.Redzynia, G.Bujacz. Crystal Structures of the Apo Form of Beta-Fructofuranosidase From Bifidobacterium Longum and Its Complex with Fructose Febs J. V. 278 1728 2011.
ISSN: ISSN 1742-464X
PubMed: 21418142
DOI: 10.1111/J.1742-4658.2011.08098.X
Page generated: Sun Jul 21 02:23:59 2024

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