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Chlorine in PDB 5fjj: Three-Dimensional Structures of Two Heavily N-Glycosylated Aspergillus Sp. Family GH3 Beta-D-Glucosidases

Enzymatic activity of Three-Dimensional Structures of Two Heavily N-Glycosylated Aspergillus Sp. Family GH3 Beta-D-Glucosidases

All present enzymatic activity of Three-Dimensional Structures of Two Heavily N-Glycosylated Aspergillus Sp. Family GH3 Beta-D-Glucosidases:
3.2.1.21;

Protein crystallography data

The structure of Three-Dimensional Structures of Two Heavily N-Glycosylated Aspergillus Sp. Family GH3 Beta-D-Glucosidases, PDB code: 5fjj was solved by J.Agirre, A.Ariza, W.A.Offen, J.P.Turkenburg, S.M.Roberts, S.Mcnicholas, P.V.Harris, B.Mcbrayer, J.Dohnalek, K.D.Cowtan, G.J.Davies, K.S.Wilson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 114.43 / 1.95
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 139.020, 141.463, 193.339, 90.00, 90.00, 90.00
R / Rfree (%) 21.565 / 25.486

Other elements in 5fjj:

The structure of Three-Dimensional Structures of Two Heavily N-Glycosylated Aspergillus Sp. Family GH3 Beta-D-Glucosidases also contains other interesting chemical elements:

Magnesium (Mg) 4 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Three-Dimensional Structures of Two Heavily N-Glycosylated Aspergillus Sp. Family GH3 Beta-D-Glucosidases (pdb code 5fjj). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Three-Dimensional Structures of Two Heavily N-Glycosylated Aspergillus Sp. Family GH3 Beta-D-Glucosidases, PDB code: 5fjj:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in 5fjj

Go back to Chlorine Binding Sites List in 5fjj
Chlorine binding site 1 out of 4 in the Three-Dimensional Structures of Two Heavily N-Glycosylated Aspergillus Sp. Family GH3 Beta-D-Glucosidases


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Three-Dimensional Structures of Two Heavily N-Glycosylated Aspergillus Sp. Family GH3 Beta-D-Glucosidases within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl6001

b:36.5
occ:1.00
 ND2 A:ASN456 3.4 27.1 1.0
NH1 A:ARG361 3.4 26.6 1.0
O A:HOH2211 3.5 45.4 1.0
CD A:ARG361 4.0 25.6 1.0
CG A:ARG361 4.0 26.4 1.0
CA A:PHE100 4.2 27.1 1.0
CD1 A:PHE100 4.2 26.3 1.0
CG A:ASN456 4.4 26.1 1.0
C A:PHE100 4.4 31.8 1.0
CZ A:ARG361 4.5 26.1 1.0
OD1 A:ASN456 4.5 24.2 1.0
NE A:ARG361 4.7 25.2 1.0
O A:SER358 4.8 29.7 1.0
CB A:PHE100 4.8 25.5 1.0
N A:SER101 4.8 32.0 1.0
O A:PHE100 4.8 32.8 1.0
O B:HOH2315 4.9 33.2 1.0
CG A:PHE100 4.9 23.5 1.0
O A:SER101 5.0 27.2 1.0

Chlorine binding site 2 out of 4 in 5fjj

Go back to Chlorine Binding Sites List in 5fjj
Chlorine binding site 2 out of 4 in the Three-Dimensional Structures of Two Heavily N-Glycosylated Aspergillus Sp. Family GH3 Beta-D-Glucosidases


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Three-Dimensional Structures of Two Heavily N-Glycosylated Aspergillus Sp. Family GH3 Beta-D-Glucosidases within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl5001

b:35.9
occ:1.00
 NH1 B:ARG361 3.4 25.9 1.0
ND2 B:ASN456 3.5 20.3 1.0
CD B:ARG361 4.1 25.5 1.0
CG B:ARG361 4.1 26.5 1.0
CD1 B:PHE100 4.2 26.8 1.0
O B:HOH2288 4.2 29.1 1.0
CA B:PHE100 4.2 21.2 1.0
C B:PHE100 4.5 21.3 1.0
CG B:ASN456 4.5 20.4 1.0
CZ B:ARG361 4.5 24.9 1.0
O B:SER358 4.6 26.4 1.0
OD1 B:ASN456 4.7 21.7 1.0
O A:HOH2322 4.7 30.4 1.0
CB B:PHE100 4.8 23.1 1.0
NE B:ARG361 4.8 25.4 1.0
O B:PHE100 4.9 21.1 1.0
N B:SER101 4.9 19.8 1.0
CG B:PHE100 4.9 23.7 1.0
CE1 B:PHE100 5.0 29.2 1.0

Chlorine binding site 3 out of 4 in 5fjj

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Chlorine binding site 3 out of 4 in the Three-Dimensional Structures of Two Heavily N-Glycosylated Aspergillus Sp. Family GH3 Beta-D-Glucosidases


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Three-Dimensional Structures of Two Heavily N-Glycosylated Aspergillus Sp. Family GH3 Beta-D-Glucosidases within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl5001

b:33.0
occ:1.00
 ND2 C:ASN456 3.4 19.3 1.0
NH1 C:ARG361 3.4 20.4 1.0
CD C:ARG361 4.0 23.4 1.0
CG C:ARG361 4.0 23.4 1.0
CA C:PHE100 4.2 18.9 1.0
CD1 C:PHE100 4.3 19.6 1.0
CG C:ASN456 4.3 22.9 1.0
O C:HOH2357 4.3 32.4 1.0
C C:PHE100 4.4 20.2 1.0
CZ C:ARG361 4.4 22.6 1.0
OD1 C:ASN456 4.5 23.5 1.0
NE C:ARG361 4.7 24.7 1.0
O C:HOH2277 4.7 35.8 1.0
N C:SER101 4.7 19.2 1.0
O D:HOH2284 4.8 26.4 1.0
CB C:PHE100 4.8 19.5 1.0
O C:SER358 4.8 18.9 1.0
O C:PHE100 4.8 18.4 1.0
O C:SER101 4.9 21.0 1.0
CG C:PHE100 5.0 18.2 1.0

Chlorine binding site 4 out of 4 in 5fjj

Go back to Chlorine Binding Sites List in 5fjj
Chlorine binding site 4 out of 4 in the Three-Dimensional Structures of Two Heavily N-Glycosylated Aspergillus Sp. Family GH3 Beta-D-Glucosidases


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Three-Dimensional Structures of Two Heavily N-Glycosylated Aspergillus Sp. Family GH3 Beta-D-Glucosidases within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl5001

b:39.4
occ:1.00
 O D:HOH2108 2.8 34.8 1.0
ND2 D:ASN456 3.2 28.0 1.0
NH1 D:ARG361 3.4 28.6 1.0
CA D:PHE100 3.9 25.7 1.0
CD1 D:PHE100 4.0 26.9 1.0
O D:HOH2255 4.0 32.5 1.0
CD D:ARG361 4.1 26.6 1.0
CG D:ASN456 4.2 26.5 1.0
CG D:ARG361 4.2 25.2 1.0
C D:PHE100 4.3 24.8 1.0
OD1 D:ASN456 4.4 24.8 1.0
CZ D:ARG361 4.5 25.6 1.0
CB D:PHE100 4.5 27.2 1.0
N D:SER101 4.6 27.6 1.0
O D:SER358 4.6 28.3 1.0
O D:PHE100 4.7 24.3 1.0
CG D:PHE100 4.7 27.8 1.0
NE D:ARG361 4.8 26.4 1.0
CE1 D:PHE100 4.8 28.3 1.0
O D:SER101 4.9 23.6 1.0
O D:HOH2050 4.9 22.2 1.0
O D:HOH2251 5.0 40.2 1.0
N D:PHE100 5.0 26.1 1.0

Reference:

J.Agirre, A.Ariza, W.A.Offen, J.P.Turkenburg, S.M.Roberts, S.Mcnicholas, P.V.Harris, B.Mcbrayer, J.Dohnalek, K.D.Cowtan, G.J.Davies, K.S.Wilson. Three-Dimensional Structures of Two Heavily N-Glycosylated Aspergillus Sp. Family GH3 Beta-D-Glucosidases Acta Crystallogr.,Sect.D V. 72 254 2016.
ISSN: ISSN 0907-4449
PubMed: 26894673
DOI: 10.1107/S2059798315024237
Page generated: Sat Dec 12 11:44:54 2020

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