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Chlorine in PDB 4qoo: Structure of Bacillus Pumilus Catalase with Resorcinol Bound.

Enzymatic activity of Structure of Bacillus Pumilus Catalase with Resorcinol Bound.

All present enzymatic activity of Structure of Bacillus Pumilus Catalase with Resorcinol Bound.:
1.11.1.6;

Protein crystallography data

The structure of Structure of Bacillus Pumilus Catalase with Resorcinol Bound., PDB code: 4qoo was solved by P.C.Loewen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 103.46 / 1.75
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 91.907, 108.597, 103.524, 90.00, 92.01, 90.00
R / Rfree (%) 17.9 / 20.9

Other elements in 4qoo:

The structure of Structure of Bacillus Pumilus Catalase with Resorcinol Bound. also contains other interesting chemical elements:

Iron (Fe) 8 atoms
Sodium (Na) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of Bacillus Pumilus Catalase with Resorcinol Bound. (pdb code 4qoo). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 6 binding sites of Chlorine where determined in the Structure of Bacillus Pumilus Catalase with Resorcinol Bound., PDB code: 4qoo:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6;

Chlorine binding site 1 out of 6 in 4qoo

Go back to Chlorine Binding Sites List in 4qoo
Chlorine binding site 1 out of 6 in the Structure of Bacillus Pumilus Catalase with Resorcinol Bound.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Bacillus Pumilus Catalase with Resorcinol Bound. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl504

b:28.9
occ:1.00
O A:HOH954 3.2 46.9 1.0
NH2 A:ARG48 3.2 18.4 1.0
NH2 B:ARG48 3.3 16.8 1.0
O D:HOH798 3.4 28.2 1.0
NE A:ARG48 3.4 18.6 1.0
NE B:ARG48 3.5 16.9 1.0
CZ A:ARG48 3.8 19.0 1.0
CZ B:ARG48 3.8 15.7 1.0
CA D:HIS346 4.1 19.7 1.0
CA C:HIS346 4.2 18.8 1.0
N D:HIS346 4.2 17.8 1.0
N C:HIS346 4.2 18.6 1.0
CB D:HIS346 4.2 21.1 1.0
CB C:HIS346 4.3 22.3 1.0
C C:ARG345 4.5 17.7 1.0
C D:ARG345 4.5 17.5 1.0
O D:ARG345 4.6 18.2 1.0
O C:ARG345 4.6 21.1 1.0
CD A:ARG48 4.6 17.2 1.0
CD B:ARG48 4.7 16.6 1.0
CB C:ARG345 4.8 16.8 1.0
CB D:ARG345 4.9 16.7 1.0

Chlorine binding site 2 out of 6 in 4qoo

Go back to Chlorine Binding Sites List in 4qoo
Chlorine binding site 2 out of 6 in the Structure of Bacillus Pumilus Catalase with Resorcinol Bound.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of Bacillus Pumilus Catalase with Resorcinol Bound. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl505

b:20.9
occ:1.00
O B:HOH638 3.1 16.6 1.0
O C:HOH697 3.2 32.6 1.0
O A:HOH613 3.3 18.7 1.0
N A:ASN367 3.4 18.8 1.0
CE C:LYS42 3.7 18.3 1.0
CB A:ASN366 3.7 17.3 1.0
CB A:ASN367 3.9 19.1 1.0
CA A:ASN367 4.0 19.5 1.0
CG C:LYS42 4.1 17.9 1.0
CD C:LYS42 4.1 18.3 1.0
N A:GLN368 4.2 18.2 1.0
C A:ASN367 4.3 19.9 1.0
CD2 C:LEU9 4.3 25.3 0.5
CG A:ASN366 4.3 18.3 1.0
C A:ASN366 4.4 19.3 1.0
CD1 C:LEU9 4.4 23.3 0.5
CD1 C:LEU9 4.4 24.6 0.5
CG A:GLN368 4.4 19.9 1.0
CA A:ASN366 4.4 17.3 1.0
NZ C:LYS42 4.4 19.3 1.0
CE1 C:HIS38 4.5 22.0 1.0
OD1 A:ASN367 4.6 22.6 1.0
OD1 A:ASN366 4.6 20.4 1.0
O B:HOH614 4.6 20.9 1.0
OD1 C:ASN20 4.7 20.9 1.0
CG A:ASN367 4.7 19.9 1.0
CG C:LEU9 4.8 25.3 0.5
CG C:LEU9 4.8 25.6 0.5
CD2 C:LEU9 4.8 25.9 0.5
OD1 B:ASP145 5.0 17.9 1.0

Chlorine binding site 3 out of 6 in 4qoo

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Chlorine binding site 3 out of 6 in the Structure of Bacillus Pumilus Catalase with Resorcinol Bound.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Structure of Bacillus Pumilus Catalase with Resorcinol Bound. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl504

b:22.5
occ:1.00
O B:HOH849 3.1 30.4 1.0
O A:HOH606 3.2 18.6 1.0
O B:HOH679 3.3 19.3 1.0
N B:ASN367 3.4 20.0 1.0
CB B:ASN366 3.7 22.3 1.0
CE D:LYS42 3.8 21.6 1.0
CB B:ASN367 3.8 22.0 1.0
CA B:ASN367 4.0 20.0 1.0
CG D:LYS42 4.1 19.9 1.0
CD D:LYS42 4.1 19.8 1.0
N B:GLN368 4.2 20.2 1.0
C B:ASN367 4.2 21.7 1.0
CG B:GLN368 4.3 22.1 1.0
CG B:ASN366 4.3 22.2 1.0
C B:ASN366 4.4 20.4 1.0
CA B:ASN366 4.4 20.9 1.0
CD1 D:LEU9 4.4 36.7 1.0
O A:HOH641 4.5 18.5 1.0
NZ D:LYS42 4.5 21.1 1.0
OD1 B:ASN367 4.6 23.2 1.0
CE1 D:HIS38 4.6 26.4 1.0
OD1 B:ASN366 4.6 21.4 1.0
CG B:ASN367 4.6 21.4 1.0
OD1 D:ASN20 4.8 22.6 1.0
CG D:LEU9 4.8 38.0 1.0
CD2 D:LEU9 4.9 43.6 1.0
O B:ASN367 4.9 21.6 1.0
NE2 B:GLN368 5.0 22.4 1.0

Chlorine binding site 4 out of 6 in 4qoo

Go back to Chlorine Binding Sites List in 4qoo
Chlorine binding site 4 out of 6 in the Structure of Bacillus Pumilus Catalase with Resorcinol Bound.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Structure of Bacillus Pumilus Catalase with Resorcinol Bound. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl504

b:26.6
occ:1.00
NH2 C:ARG48 3.1 19.0 1.0
NH2 D:ARG48 3.2 21.4 1.0
NE C:ARG48 3.4 16.2 1.0
NE D:ARG48 3.5 19.5 1.0
O B:HOH821 3.6 33.6 1.0
O A:HOH875 3.7 34.9 1.0
CZ C:ARG48 3.7 16.1 1.0
CZ D:ARG48 3.8 20.7 1.0
CA B:HIS346 4.1 19.3 1.0
N B:HIS346 4.1 20.7 1.0
N A:HIS346 4.2 17.4 1.0
CA A:HIS346 4.2 19.3 1.0
CB B:HIS346 4.3 21.3 1.0
CB A:HIS346 4.3 21.5 1.0
C A:ARG345 4.5 17.1 1.0
C B:ARG345 4.5 20.5 1.0
O A:ARG345 4.6 19.1 1.0
CD C:ARG48 4.6 16.1 1.0
O B:ARG345 4.7 22.1 1.0
CD D:ARG48 4.7 18.8 1.0
CB A:ARG345 4.8 19.4 1.0
CB B:ARG345 4.8 19.4 1.0

Chlorine binding site 5 out of 6 in 4qoo

Go back to Chlorine Binding Sites List in 4qoo
Chlorine binding site 5 out of 6 in the Structure of Bacillus Pumilus Catalase with Resorcinol Bound.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Structure of Bacillus Pumilus Catalase with Resorcinol Bound. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl505

b:23.7
occ:1.00
O C:HOH681 3.1 32.9 1.0
O D:HOH680 3.1 21.0 1.0
O C:HOH620 3.3 19.2 1.0
N C:ASN367 3.3 18.0 1.0
CE A:LYS42 3.7 19.0 1.0
CB C:ASN366 3.7 18.9 1.0
CB C:ASN367 3.8 19.7 1.0
CA C:ASN367 4.0 19.1 1.0
CG A:LYS42 4.0 18.7 1.0
CD A:LYS42 4.0 18.7 1.0
N C:GLN368 4.1 18.2 1.0
C C:ASN367 4.2 19.6 1.0
C C:ASN366 4.4 20.3 1.0
CG C:GLN368 4.4 19.7 1.0
CG C:ASN366 4.4 19.1 1.0
NZ A:LYS42 4.4 19.5 1.0
O D:HOH625 4.4 19.2 1.0
CA C:ASN366 4.5 19.1 1.0
CD1 A:LEU9 4.5 32.0 1.0
OD1 C:ASN367 4.5 23.5 1.0
CG C:ASN367 4.6 20.9 1.0
OD1 C:ASN366 4.6 22.1 1.0
CE1 A:HIS38 4.6 19.1 1.0
OD1 A:ASN20 4.7 19.8 1.0
CG A:LEU9 4.9 36.8 1.0
CD2 A:LEU9 4.9 42.5 1.0
O C:ASN367 4.9 19.3 1.0

Chlorine binding site 6 out of 6 in 4qoo

Go back to Chlorine Binding Sites List in 4qoo
Chlorine binding site 6 out of 6 in the Structure of Bacillus Pumilus Catalase with Resorcinol Bound.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of Structure of Bacillus Pumilus Catalase with Resorcinol Bound. within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl504

b:20.4
occ:1.00
O D:HOH632 3.1 32.5 1.0
O C:HOH605 3.1 20.4 1.0
O D:HOH677 3.2 17.2 1.0
N D:ASN367 3.3 18.3 1.0
CB D:ASN366 3.7 18.6 1.0
CE B:LYS42 3.8 18.7 1.0
CB D:ASN367 3.9 18.0 1.0
CA D:ASN367 4.0 18.5 1.0
CG B:LYS42 4.1 17.8 1.0
CD B:LYS42 4.1 18.9 1.0
N D:GLN368 4.2 17.9 1.0
C D:ASN367 4.2 17.6 1.0
C D:ASN366 4.3 20.1 1.0
CG D:ASN366 4.4 20.7 1.0
CA D:ASN366 4.4 19.5 1.0
CG D:GLN368 4.4 18.9 1.0
CD1 B:LEU9 4.5 30.8 1.0
NZ B:LYS42 4.5 19.8 1.0
OD1 D:ASN367 4.6 22.1 1.0
OD1 D:ASN366 4.6 18.6 1.0
O C:HOH638 4.6 20.9 1.0
CE1 B:HIS38 4.6 20.8 1.0
CG D:ASN367 4.6 18.6 1.0
OD1 B:ASN20 4.7 23.5 1.0
CG B:LEU9 4.8 31.6 1.0
CD2 B:LEU9 4.9 34.9 1.0
O D:ASN367 4.9 19.5 1.0

Reference:

P.C.Loewen, J.Villanueva, J.Switala, L.J.Donald, A.Ivancich. Unprecedented Access of Phenolic Substrates to the Heme Active Site of A Catalase: Substrate Binding and Peroxidase-Like Reactivity of Bacillus Pumilus Catalase Monitored By X-Ray Crystallography and Epr Spectroscopy. Proteins 2015.
ISSN: ESSN 1097-0134
PubMed: 25663126
DOI: 10.1002/PROT.24777
Page generated: Sat Dec 12 11:06:12 2020

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