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Chlorine in PDB 5fip: Discovery and Characterization of A Novel Thermostable and Highly Halotolerant GH5 Cellulase From An Icelandic Hot Spring Isolate

Enzymatic activity of Discovery and Characterization of A Novel Thermostable and Highly Halotolerant GH5 Cellulase From An Icelandic Hot Spring Isolate

All present enzymatic activity of Discovery and Characterization of A Novel Thermostable and Highly Halotolerant GH5 Cellulase From An Icelandic Hot Spring Isolate:
3.2.1.4;

Protein crystallography data

The structure of Discovery and Characterization of A Novel Thermostable and Highly Halotolerant GH5 Cellulase From An Icelandic Hot Spring Isolate, PDB code: 5fip was solved by D.Zarafeta, D.Kissas, C.Sayer, S.R.Gudbergsdottir, E.Ladoukakis, M.N.Isupov, A.Chatziioannou, X.Peng, J.A.Littlechild, G.Skretas, F.N.Kolisis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.38 / 1.88
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 107.340, 137.450, 121.340, 90.00, 114.44, 90.00
R / Rfree (%) 19.31 / 23.393

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Discovery and Characterization of A Novel Thermostable and Highly Halotolerant GH5 Cellulase From An Icelandic Hot Spring Isolate (pdb code 5fip). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 7 binding sites of Chlorine where determined in the Discovery and Characterization of A Novel Thermostable and Highly Halotolerant GH5 Cellulase From An Icelandic Hot Spring Isolate, PDB code: 5fip:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6; 7;

Chlorine binding site 1 out of 7 in 5fip

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Chlorine binding site 1 out of 7 in the Discovery and Characterization of A Novel Thermostable and Highly Halotolerant GH5 Cellulase From An Icelandic Hot Spring Isolate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Discovery and Characterization of A Novel Thermostable and Highly Halotolerant GH5 Cellulase From An Icelandic Hot Spring Isolate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1396

b:53.2
occ:0.90
 N A:TYR375 3.1 42.4 1.0
NH1 A:ARG369 3.4 33.8 1.0
NH2 A:ARG369 3.4 36.3 1.0
CA A:PRO374 3.7 39.8 1.0
CZ A:ARG369 3.9 35.3 1.0
CB A:TYR375 3.9 44.3 1.0
C A:PRO374 3.9 44.4 1.0
CA A:TYR375 4.0 42.8 1.0
O A:TYR375 4.3 39.3 1.0
CB A:PRO374 4.4 48.0 1.0
C A:TYR375 4.7 47.6 1.0
O A:ILE373 4.8 42.1 1.0
N A:PRO374 4.9 48.4 1.0

Chlorine binding site 2 out of 7 in 5fip

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Chlorine binding site 2 out of 7 in the Discovery and Characterization of A Novel Thermostable and Highly Halotolerant GH5 Cellulase From An Icelandic Hot Spring Isolate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Discovery and Characterization of A Novel Thermostable and Highly Halotolerant GH5 Cellulase From An Icelandic Hot Spring Isolate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1397

b:30.6
occ:0.50
 OE2 A:GLU197 2.1 33.3 0.5
CD A:GLU197 3.0 38.2 0.5
OE1 A:GLU197 3.3 46.4 0.5
O A:HOH2087 3.5 58.8 1.0
OE2 A:GLU197 3.6 33.4 0.5
CD A:GLU197 4.1 36.0 0.5
CG A:GLU197 4.4 33.3 0.5
CG A:GLU197 4.4 34.6 0.5
OE1 A:GLU197 4.9 32.0 0.5

Chlorine binding site 3 out of 7 in 5fip

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Chlorine binding site 3 out of 7 in the Discovery and Characterization of A Novel Thermostable and Highly Halotolerant GH5 Cellulase From An Icelandic Hot Spring Isolate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Discovery and Characterization of A Novel Thermostable and Highly Halotolerant GH5 Cellulase From An Icelandic Hot Spring Isolate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1400

b:59.1
occ:0.80
 O A:HOH2157 3.0 59.5 1.0
NH2 A:ARG278 3.5 34.9 0.5
CD C:LYS282 4.0 42.3 1.0
ND2 C:ASN286 4.0 38.2 1.0
CE C:LYS282 4.1 52.7 1.0
NZ C:LYS282 4.4 71.8 1.0
CZ A:ARG278 4.6 36.1 0.5
CG C:LYS282 4.7 38.5 1.0
NE A:ARG278 4.8 32.2 0.5
NH1 A:ARG278 4.9 34.5 0.5
OD1 C:ASN286 4.9 43.3 1.0
CG C:ASN286 4.9 46.4 1.0
CD A:ARG278 5.0 46.0 0.5

Chlorine binding site 4 out of 7 in 5fip

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Chlorine binding site 4 out of 7 in the Discovery and Characterization of A Novel Thermostable and Highly Halotolerant GH5 Cellulase From An Icelandic Hot Spring Isolate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Discovery and Characterization of A Novel Thermostable and Highly Halotolerant GH5 Cellulase From An Icelandic Hot Spring Isolate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl1400

b:47.3
occ:1.00
 N B:TYR375 3.3 32.3 1.0
NH2 B:ARG369 3.4 31.5 1.0
NH1 B:ARG369 3.5 35.1 1.0
CA B:PRO374 3.8 37.1 1.0
CZ B:ARG369 3.9 31.4 1.0
CB B:TYR375 4.1 31.2 1.0
C B:PRO374 4.1 30.8 1.0
CA B:TYR375 4.3 37.7 1.0
CB B:PRO374 4.3 37.2 1.0
O B:TYR375 4.5 38.2 1.0
C B:TYR375 4.8 31.4 1.0
O B:ILE373 5.0 37.7 1.0

Chlorine binding site 5 out of 7 in 5fip

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Chlorine binding site 5 out of 7 in the Discovery and Characterization of A Novel Thermostable and Highly Halotolerant GH5 Cellulase From An Icelandic Hot Spring Isolate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Discovery and Characterization of A Novel Thermostable and Highly Halotolerant GH5 Cellulase From An Icelandic Hot Spring Isolate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl1401

b:39.9
occ:0.70
 O B:HOH2163 2.6 56.0 1.0
N B:GLU310 3.3 29.0 1.0
C B:TYR307 3.5 36.2 1.0
N B:ASN309 3.5 32.5 1.0
CB B:TYR307 3.5 31.1 1.0
CA B:TYR307 3.6 24.8 1.0
CB B:ASN309 3.7 32.4 0.5
N B:LEU308 3.7 25.4 1.0
CB B:ASN309 3.9 33.3 0.5
CB B:GLU310 3.9 32.5 1.0
O B:TYR307 3.9 28.9 1.0
CA B:ASN309 4.0 32.2 0.5
CA B:ASN309 4.0 31.8 0.5
CD2 B:TYR307 4.0 42.3 1.0
C B:ASN309 4.1 33.0 1.0
CA B:GLU310 4.2 30.5 1.0
CG B:TYR307 4.3 33.6 1.0
C B:LEU308 4.4 31.2 1.0
CA B:LEU308 4.6 26.4 1.0
O B:HOH2162 4.6 38.5 1.0
OD1 B:ASN309 4.6 39.0 0.5
OD1 B:ASN309 4.7 41.2 0.5
CG B:ASN309 4.7 32.9 0.5
CG B:ASN309 4.7 34.1 0.5

Chlorine binding site 6 out of 7 in 5fip

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Chlorine binding site 6 out of 7 in the Discovery and Characterization of A Novel Thermostable and Highly Halotolerant GH5 Cellulase From An Icelandic Hot Spring Isolate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of Discovery and Characterization of A Novel Thermostable and Highly Halotolerant GH5 Cellulase From An Icelandic Hot Spring Isolate within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl1385

b:56.4
occ:0.80
 N C:TYR375 3.3 48.3 1.0
NH1 C:ARG369 3.5 46.4 1.0
NH2 C:ARG369 3.7 34.1 1.0
CB C:TYR375 3.9 52.6 1.0
CA C:PRO374 4.0 55.1 1.0
CZ C:ARG369 4.0 38.4 1.0
C C:PRO374 4.1 57.3 1.0
CA C:TYR375 4.1 51.9 1.0
O C:TYR375 4.5 70.3 1.0
CB C:PRO374 4.7 52.7 1.0
C C:TYR375 4.8 66.0 1.0

Chlorine binding site 7 out of 7 in 5fip

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Chlorine binding site 7 out of 7 in the Discovery and Characterization of A Novel Thermostable and Highly Halotolerant GH5 Cellulase From An Icelandic Hot Spring Isolate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 7 of Discovery and Characterization of A Novel Thermostable and Highly Halotolerant GH5 Cellulase From An Icelandic Hot Spring Isolate within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl1395

b:52.2
occ:0.70
 NH1 D:ARG369 3.4 48.1 1.0
N D:TYR375 3.4 55.2 1.0
NH2 D:ARG369 3.6 40.3 1.0
CA D:PRO374 3.9 63.0 1.0
CZ D:ARG369 3.9 44.9 1.0
C D:PRO374 4.2 64.3 1.0
CB D:TYR375 4.3 56.2 1.0
CA D:TYR375 4.3 56.9 1.0
CB D:PRO374 4.3 58.0 1.0
O D:TYR375 4.5 55.4 1.0
C D:TYR375 4.9 56.2 1.0

Reference:

D.Zarafeta, D.Kissas, C.Sayer, S.R.Gudbergsdottir, E.Ladoukakis, M.N.Isupov, A.Chatziioannou, X.Peng, J.A.Littlechild, G.Skretas, F.N.Kolisis. Discovery and Characterization of A Thermostable and Highly Halotolerant GH5 Cellulase From An Icelandic Hot Spring Isolate. Plos One V. 11 46454 2016.
ISSN: ISSN 1932-6203
PubMed: 26741138
DOI: 10.1371/JOURNAL.PONE.0146454
Page generated: Sat Jul 12 02:07:10 2025

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