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Chlorine in PDB 1itk: Crystal Structure of Catalase-Peroxidase From Haloarcula Marismortui

Enzymatic activity of Crystal Structure of Catalase-Peroxidase From Haloarcula Marismortui

All present enzymatic activity of Crystal Structure of Catalase-Peroxidase From Haloarcula Marismortui:
1.11.1.6;

Protein crystallography data

The structure of Crystal Structure of Catalase-Peroxidase From Haloarcula Marismortui, PDB code: 1itk was solved by Y.Yamada, T.Fujiwara, T.Sato, N.Igarashi, N.Tanaka, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.10 / 2.00
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 317.632, 82.141, 75.102, 90.00, 100.24, 90.00
R / Rfree (%) 18.2 / 20.3

Other elements in 1itk:

The structure of Crystal Structure of Catalase-Peroxidase From Haloarcula Marismortui also contains other interesting chemical elements:

Iron (Fe) 2 atoms

Chlorine Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 16;

Binding sites:

The binding sites of Chlorine atom in the Crystal Structure of Catalase-Peroxidase From Haloarcula Marismortui (pdb code 1itk). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 16 binding sites of Chlorine where determined in the Crystal Structure of Catalase-Peroxidase From Haloarcula Marismortui, PDB code: 1itk:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Chlorine binding site 1 out of 16 in 1itk

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Chlorine binding site 1 out of 16 in the Crystal Structure of Catalase-Peroxidase From Haloarcula Marismortui


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Catalase-Peroxidase From Haloarcula Marismortui within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl2001

b:16.0
occ:1.00
OG A:SER212 3.1 14.4 1.0
O A:HOH2200 3.2 18.8 1.0
ND2 A:ASN236 3.3 12.3 1.0
O A:HOH2044 3.3 17.9 1.0
N A:ASN220 3.3 14.9 1.0
CA A:PRO224 3.6 16.6 1.0
CB A:ASN220 3.7 14.3 1.0
CB A:VAL219 3.7 13.2 1.0
N A:PRO224 3.9 17.0 1.0
CB A:SER212 3.9 13.7 1.0
CB A:ASN236 4.0 14.5 1.0
CA A:ASN220 4.1 13.6 1.0
CG A:ASN236 4.1 16.0 1.0
CB A:PRO224 4.1 16.4 1.0
CA A:VAL219 4.1 12.9 1.0
CG A:PRO224 4.2 20.8 1.0
C A:VAL219 4.2 13.8 1.0
C A:GLY223 4.3 16.7 1.0
O A:GLY223 4.3 17.8 1.0
CG1 A:VAL219 4.3 12.7 1.0
O A:ASN220 4.4 10.5 1.0
CD A:PRO224 4.7 17.2 1.0
CG2 A:VAL213 4.7 15.9 1.0
CZ A:PHE199 4.7 15.9 1.0
CE2 A:PHE199 4.7 17.5 1.0
C A:ASN220 4.7 11.8 1.0
C A:PRO224 4.8 17.3 1.0
CG2 A:VAL219 4.8 13.0 1.0
N A:ASP225 4.8 15.9 1.0

Chlorine binding site 2 out of 16 in 1itk

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Chlorine binding site 2 out of 16 in the Crystal Structure of Catalase-Peroxidase From Haloarcula Marismortui


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Catalase-Peroxidase From Haloarcula Marismortui within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl2002

b:18.6
occ:1.00
OG A:SER612 3.1 16.3 1.0
O A:HOH2045 3.2 19.2 1.0
O B:HOH2221 3.2 24.4 1.0
N B:GLY44 3.2 18.4 1.0
N A:SER612 3.3 15.8 1.0
O A:HOH2120 3.4 18.0 1.0
CB A:SER612 3.7 16.6 1.0
N A:ALA611 3.8 14.3 1.0
CB A:ALA611 3.9 12.8 1.0
CB B:VAL43 4.0 22.0 1.0
CB A:THR610 4.1 17.2 1.0
CA A:SER612 4.1 15.8 1.0
CA B:GLY44 4.1 18.1 1.0
CA B:VAL43 4.1 21.6 1.0
CA A:ALA611 4.1 14.3 1.0
C A:ALA611 4.2 14.6 1.0
C B:VAL43 4.2 20.5 1.0
OG1 A:THR610 4.3 16.9 1.0
O B:GLY44 4.3 15.4 1.0
C B:GLY44 4.4 18.4 1.0
O A:HOH2117 4.6 15.6 1.0
CD1 A:ILE698 4.6 15.7 1.0
CG1 B:VAL43 4.6 21.8 1.0
C A:THR610 4.6 16.9 1.0
NH2 A:ARG694 4.7 17.2 1.0
OD1 A:ASP37 4.9 17.4 1.0
CA A:THR610 4.9 16.8 1.0

Chlorine binding site 3 out of 16 in 1itk

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Chlorine binding site 3 out of 16 in the Crystal Structure of Catalase-Peroxidase From Haloarcula Marismortui


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of Catalase-Peroxidase From Haloarcula Marismortui within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl2004

b:22.4
occ:1.00
O A:HOH2155 3.1 21.8 1.0
N A:GLY583 3.2 17.6 1.0
ND2 A:ASN603 3.3 16.6 1.0
O A:HOH2173 3.3 19.2 1.0
CB A:ASN603 3.4 15.2 1.0
O A:HOH2472 3.5 29.7 1.0
CA A:ASP582 3.6 18.5 1.0
O A:VAL581 3.6 15.7 1.0
O A:HOH2446 3.8 31.8 1.0
CG A:ASN603 3.9 17.2 1.0
C A:ASP582 3.9 17.2 1.0
CD1 A:LEU600 4.0 15.0 1.0
C A:VAL581 4.2 17.9 1.0
CA A:GLY583 4.2 17.5 1.0
N A:ASP582 4.2 17.3 1.0
O A:HOH2259 4.3 27.5 1.0
O A:LEU600 4.5 14.4 1.0
OD1 A:ASP582 4.6 20.4 1.0
CA A:LEU600 4.6 14.4 1.0
CG1 A:VAL581 4.6 19.5 1.0
CB A:ASP582 4.7 17.7 1.0
CG A:ASP582 4.8 18.6 1.0
CA A:ASN603 4.8 14.0 1.0
O A:HOH2089 4.9 15.2 1.0

Chlorine binding site 4 out of 16 in 1itk

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Chlorine binding site 4 out of 16 in the Crystal Structure of Catalase-Peroxidase From Haloarcula Marismortui


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of Catalase-Peroxidase From Haloarcula Marismortui within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl2005

b:20.8
occ:1.00
NZ A:LYS376 3.2 15.6 1.0
NH2 A:ARG377 3.2 23.8 1.0
N A:TRP331 3.3 18.1 1.0
CE A:LYS376 3.6 16.0 1.0
CD A:LYS376 3.8 15.6 1.0
CD1 A:TRP331 3.9 15.8 1.0
NE A:ARG377 3.9 20.0 1.0
O A:TYR329 4.0 18.0 1.0
CA A:GLU330 4.0 22.2 1.0
CZ A:ARG377 4.0 22.6 1.0
CB A:TRP331 4.0 15.8 1.0
C A:GLU330 4.1 21.0 1.0
CA A:TRP331 4.1 17.4 1.0
O A:TRP331 4.2 16.1 1.0
CG A:TRP331 4.4 14.6 1.0
C A:TRP331 4.6 16.3 1.0
O A:HOH2360 4.8 22.5 1.0
CB A:GLU330 4.9 27.1 1.0
C A:TYR329 4.9 20.4 1.0
CG A:LYS376 4.9 16.1 1.0
N A:GLU330 5.0 21.1 1.0
CD1 A:ILE373 5.0 14.1 1.0

Chlorine binding site 5 out of 16 in 1itk

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Chlorine binding site 5 out of 16 in the Crystal Structure of Catalase-Peroxidase From Haloarcula Marismortui


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Crystal Structure of Catalase-Peroxidase From Haloarcula Marismortui within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl2006

b:28.1
occ:1.00
O A:HOH2319 2.9 23.6 1.0
N A:ALA571 3.1 14.0 1.0
O A:HOH2086 3.1 18.4 1.0
O A:THR569 3.3 14.3 1.0
CB A:ALA571 3.4 15.4 1.0
O A:HOH2197 3.6 23.5 1.0
CD A:PRO572 3.7 14.8 1.0
CA A:ALA571 3.8 14.5 1.0
C A:ASP570 3.9 14.9 1.0
CA A:ASP570 3.9 14.9 1.0
C A:THR569 4.3 14.8 1.0
OD1 A:ASP570 4.6 19.6 1.0
N A:ASP570 4.6 14.9 1.0
N A:PRO572 4.7 16.3 1.0
C A:ALA571 4.8 15.2 1.0
CG A:PRO572 4.8 16.5 1.0

Chlorine binding site 6 out of 16 in 1itk

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Chlorine binding site 6 out of 16 in the Crystal Structure of Catalase-Peroxidase From Haloarcula Marismortui


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of Crystal Structure of Catalase-Peroxidase From Haloarcula Marismortui within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl2007

b:22.2
occ:1.00
N B:LYS21 3.1 30.3 1.0
N A:TRP187 3.1 16.3 1.0
O B:HOH2033 3.2 19.8 1.0
O A:HOH2576 3.3 19.6 1.0
CA B:PRO20 3.7 32.2 1.0
CB A:TRP187 3.8 14.0 1.0
CB B:LYS21 3.9 29.8 1.0
CA A:TRP187 3.9 16.4 1.0
C B:PRO20 3.9 31.8 1.0
OD1 A:ASN186 3.9 22.0 1.0
C A:ASN186 4.0 17.6 1.0
CA B:LYS21 4.0 29.6 1.0
CA A:ASN186 4.0 19.5 1.0
N A:GLY188 4.0 17.9 1.0
O A:GLY188 4.1 18.4 1.0
CD1 A:TRP187 4.1 13.9 1.0
O A:VAL185 4.2 17.9 1.0
O B:LYS21 4.2 28.9 1.0
CB B:PRO20 4.3 32.5 1.0
CG A:TRP187 4.3 14.3 1.0
C A:TRP187 4.4 16.7 1.0
O A:HOH2405 4.4 31.4 1.0
CE A:MET214 4.4 13.7 1.0
CG A:ASN186 4.6 23.9 1.0
C B:LYS21 4.6 28.5 1.0
O A:HOH2041 4.8 14.7 1.0
CB A:ASN186 5.0 19.9 1.0
O B:ARG19 5.0 33.1 1.0

Chlorine binding site 7 out of 16 in 1itk

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Chlorine binding site 7 out of 16 in the Crystal Structure of Catalase-Peroxidase From Haloarcula Marismortui


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 7 of Crystal Structure of Catalase-Peroxidase From Haloarcula Marismortui within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl2009

b:24.6
occ:1.00
O A:HOH2591 3.1 36.0 1.0
O A:HOH2152 3.1 21.7 1.0
N A:GLU47 3.2 25.2 1.0
NE2 A:GLN145 3.2 22.5 1.0
O B:HOH2410 3.4 29.7 1.0
NZ B:LYS710 3.6 23.8 1.0
CA A:VAL46 3.8 21.4 1.0
CG A:GLU47 3.8 35.7 1.0
CB A:GLU47 3.8 30.7 1.0
CG1 A:VAL46 3.9 21.6 1.0
OE1 A:GLN145 4.0 26.2 1.0
C A:VAL46 4.0 22.3 1.0
CD A:GLN145 4.0 22.6 1.0
CE B:LYS710 4.1 22.5 1.0
CA A:GLU47 4.1 28.4 1.0
CB A:PHE50 4.2 25.6 1.0
O A:HOH2693 4.2 31.9 1.0
CG A:PHE50 4.3 24.5 1.0
CD B:LYS710 4.4 24.4 1.0
CB A:VAL46 4.4 21.6 1.0
CD1 A:PHE50 4.4 24.2 1.0
O A:PRO45 4.5 20.5 1.0
O B:HOH2607 4.7 41.9 1.0
N A:VAL46 4.8 19.4 1.0
CG2 A:VAL46 4.9 20.0 1.0
O A:GLU47 4.9 26.9 1.0
O A:HOH2268 4.9 22.5 1.0
O B:HOH2269 4.9 29.8 1.0

Chlorine binding site 8 out of 16 in 1itk

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Chlorine binding site 8 out of 16 in the Crystal Structure of Catalase-Peroxidase From Haloarcula Marismortui


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 8 of Crystal Structure of Catalase-Peroxidase From Haloarcula Marismortui within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl2010

b:27.5
occ:1.00
N B:TRP187 3.1 18.6 1.0
N A:LYS21 3.2 31.8 1.0
O A:HOH2175 3.2 18.1 1.0
O B:HOH2415 3.4 26.2 1.0
CB B:TRP187 3.8 19.8 1.0
CA A:PRO20 3.9 34.9 1.0
CB A:LYS21 3.9 31.1 1.0
CA B:TRP187 3.9 20.0 1.0
OD1 B:ASN186 3.9 25.3 1.0
C B:ASN186 4.0 20.7 1.0
C A:PRO20 4.0 33.4 1.0
CA B:ASN186 4.0 21.2 1.0
N B:GLY188 4.1 22.5 1.0
CA A:LYS21 4.1 32.3 1.0
CD1 B:TRP187 4.1 20.7 1.0
O B:GLY188 4.2 25.9 1.0
O B:VAL185 4.2 21.1 1.0
O A:LYS21 4.2 32.5 1.0
CG B:TRP187 4.3 22.0 1.0
C B:TRP187 4.3 20.7 1.0
CE B:MET214 4.4 21.6 1.0
CB A:PRO20 4.5 35.7 1.0
CG B:ASN186 4.5 27.0 1.0
C A:LYS21 4.7 31.6 1.0
O B:HOH2298 4.9 24.6 1.0
CB B:ASN186 4.9 23.8 1.0
O A:ARG19 4.9 37.3 1.0

Chlorine binding site 9 out of 16 in 1itk

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Chlorine binding site 9 out of 16 in the Crystal Structure of Catalase-Peroxidase From Haloarcula Marismortui


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 9 of Crystal Structure of Catalase-Peroxidase From Haloarcula Marismortui within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl2011

b:28.2
occ:1.00
O A:HOH2129 3.1 17.3 1.0
N A:GLU491 3.2 16.0 1.0
CG A:GLU491 3.7 24.3 1.0
CB A:GLU491 3.8 20.1 1.0
CB A:LEU490 3.8 16.1 1.0
CB A:PRO566 3.8 19.2 1.0
CA A:LEU490 4.0 16.2 1.0
CD2 A:LEU490 4.1 14.7 1.0
CA A:GLU491 4.1 17.5 1.0
C A:LEU490 4.1 17.5 1.0
CG A:LEU490 4.5 16.0 1.0
CA A:PRO566 4.6 17.0 1.0
CG A:PRO566 4.6 19.6 1.0
O A:GLU491 4.6 14.3 1.0
O A:HOH2086 4.6 18.4 1.0
O A:HOH2284 4.7 28.4 1.0
CD A:PRO566 4.9 17.6 1.0
C A:GLU491 4.9 15.6 1.0
CD1 A:LEU490 4.9 16.7 1.0

Chlorine binding site 10 out of 16 in 1itk

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Chlorine binding site 10 out of 16 in the Crystal Structure of Catalase-Peroxidase From Haloarcula Marismortui


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 10 of Crystal Structure of Catalase-Peroxidase From Haloarcula Marismortui within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl2012

b:28.8
occ:1.00
O A:HOH2057 2.9 17.9 1.0
O A:HOH2062 3.0 18.6 1.0
NH1 A:ARG487 3.0 16.7 1.0
O A:HOH2169 3.1 15.5 1.0
O A:HOH2063 3.4 19.3 1.0
CA A:GLY481 3.4 15.5 1.0
CE2 A:PHE574 3.6 16.4 1.0
C A:GLY481 3.7 15.8 1.0
N A:GLY481 3.7 15.8 1.0
CD A:ARG487 3.9 16.9 1.0
O A:HOH2049 3.9 16.1 1.0
CZ A:PHE574 3.9 13.3 1.0
O A:GLY481 4.0 15.8 1.0
O A:GLY482 4.1 14.4 1.0
CZ A:ARG487 4.1 17.4 1.0
N A:GLY482 4.1 15.0 1.0
O A:ASN484 4.2 19.4 1.0
CG A:ARG487 4.3 17.7 1.0
NE A:ARG487 4.4 15.1 1.0
CB A:ARG487 4.6 16.7 1.0
O A:HOH2222 4.6 20.1 1.0
CD2 A:PHE574 4.8 14.1 1.0
C A:GLY482 4.9 16.1 1.0
CA A:GLY482 5.0 16.6 1.0
C A:ARG480 5.0 16.1 1.0

Reference:

Y.Yamada, T.Fujiwara, T.Sato, N.Igarashi, N.Tanaka. The 2.0 A Crystal Structure of Catalase-Peroxidase From Haloarcula Marismortui. Nat.Struct.Biol. V. 9 691 2002.
ISSN: ISSN 1072-8368
PubMed: 12172540
DOI: 10.1038/NSB834
Page generated: Sat Dec 12 08:38:15 2020

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