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Chlorine in PDB 4wfj: Crystal Structure of Pet-Degrading Cutinase CUT190 S226P Mutant in Ca(2+)-Bound State at 1.75 Angstrom Resolution

Protein crystallography data

The structure of Crystal Structure of Pet-Degrading Cutinase CUT190 S226P Mutant in Ca(2+)-Bound State at 1.75 Angstrom Resolution, PDB code: 4wfj was solved by T.Miyakawa, H.Mizushima, J.Ohtsuka, M.Oda, F.Kawai, M.Tanokura, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.55 / 1.75
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 54.560, 65.840, 70.080, 90.00, 90.00, 90.00
R / Rfree (%) 20.3 / 24.5

Other elements in 4wfj:

The structure of Crystal Structure of Pet-Degrading Cutinase CUT190 S226P Mutant in Ca(2+)-Bound State at 1.75 Angstrom Resolution also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Pet-Degrading Cutinase CUT190 S226P Mutant in Ca(2+)-Bound State at 1.75 Angstrom Resolution (pdb code 4wfj). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Pet-Degrading Cutinase CUT190 S226P Mutant in Ca(2+)-Bound State at 1.75 Angstrom Resolution, PDB code: 4wfj:

Chlorine binding site 1 out of 1 in 4wfj

Go back to Chlorine Binding Sites List in 4wfj
Chlorine binding site 1 out of 1 in the Crystal Structure of Pet-Degrading Cutinase CUT190 S226P Mutant in Ca(2+)-Bound State at 1.75 Angstrom Resolution


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 Pet-Degrading Cutinase CUT190 S226P Mutant in Ca(2+)-Bound State at 1.75 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl402

b:37.3
occ:1.00
O A:ASP222 2.9 22.8 1.0
O A:GLU220 2.9 26.4 1.0
N A:VAL227 3.0 21.5 1.0
O A:HOH545 3.2 27.3 1.0
O A:ALA219 3.3 23.5 1.0
N A:ASP222 3.3 25.0 1.0
CG2 A:VAL227 3.4 20.2 1.0
CA A:PRO226 3.6 24.9 1.0
CB A:ASP222 3.7 24.6 1.0
C A:GLU220 3.7 27.1 1.0
CG1 A:VAL227 3.7 22.6 1.0
C A:ASP222 3.7 25.4 1.0
CA A:ASP222 3.7 22.1 1.0
C A:PRO226 3.7 20.5 1.0
CB A:VAL227 3.8 20.7 1.0
CA A:VAL227 4.0 22.6 1.0
C A:LEU221 4.1 24.0 1.0
CB A:PRO226 4.3 24.6 1.0
N A:LEU221 4.3 26.7 1.0
C A:ALA219 4.4 18.9 1.0
CA A:LEU221 4.5 22.6 1.0
CA A:GLU220 4.5 23.0 1.0
N A:PRO226 4.7 21.9 1.0
O A:ALA225 4.8 21.4 1.0
N A:ARG228 4.9 23.1 1.0
O A:LEU221 4.9 28.4 1.0
CG A:ASP222 4.9 23.8 1.0
N A:GLU220 4.9 20.4 1.0
O A:PRO226 4.9 21.3 1.0
N A:THR223 5.0 22.0 1.0
C A:VAL227 5.0 22.4 1.0

Reference:

T.Miyakawa, H.Mizushima, J.Ohtsuka, M.Oda, F.Kawai, M.Tanokura. Structural Basis For the Ca(2+)-Enhanced Thermostability and Activity of Pet-Degrading Cutinase-Like Enzyme From Saccharomonospora Viridis AHK190. Appl.Microbiol.Biotechnol. 2014.
ISSN: ESSN 1432-0614
PubMed: 25492421
DOI: 10.1007/S00253-014-6272-8
Page generated: Fri Jul 11 22:30:24 2025

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