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Chlorine in PDB 1w5m: Stepwise Introduction of Zinc Binding Site Into Porphobilinogen Synthase of Pseudomonas Aeruginosa (Mutations A129C and D139C)

Enzymatic activity of Stepwise Introduction of Zinc Binding Site Into Porphobilinogen Synthase of Pseudomonas Aeruginosa (Mutations A129C and D139C)

All present enzymatic activity of Stepwise Introduction of Zinc Binding Site Into Porphobilinogen Synthase of Pseudomonas Aeruginosa (Mutations A129C and D139C):
4.2.1.24;

Protein crystallography data

The structure of Stepwise Introduction of Zinc Binding Site Into Porphobilinogen Synthase of Pseudomonas Aeruginosa (Mutations A129C and D139C), PDB code: 1w5m was solved by F.Frere, H.Reents, W.-D.Schubert, D.W.Heinz, D.Jahn, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 87.71 / 1.60
Space group P 4 21 2
Cell size a, b, c (Å), α, β, γ (°) 126.307, 126.307, 85.156, 90.00, 90.00, 90.00
R / Rfree (%) 12.9 / 16.5

Other elements in 1w5m:

The structure of Stepwise Introduction of Zinc Binding Site Into Porphobilinogen Synthase of Pseudomonas Aeruginosa (Mutations A129C and D139C) also contains other interesting chemical elements:

Magnesium (Mg) 7 atoms
Zinc (Zn) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Stepwise Introduction of Zinc Binding Site Into Porphobilinogen Synthase of Pseudomonas Aeruginosa (Mutations A129C and D139C) (pdb code 1w5m). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Stepwise Introduction of Zinc Binding Site Into Porphobilinogen Synthase of Pseudomonas Aeruginosa (Mutations A129C and D139C), PDB code: 1w5m:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 1w5m

Go back to Chlorine Binding Sites List in 1w5m
Chlorine binding site 1 out of 2 in the Stepwise Introduction of Zinc Binding Site Into Porphobilinogen Synthase of Pseudomonas Aeruginosa (Mutations A129C and D139C)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Stepwise Introduction of Zinc Binding Site Into Porphobilinogen Synthase of Pseudomonas Aeruginosa (Mutations A129C and D139C) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1337

b:25.4
occ:0.80
N A:VAL32 3.1 11.9 1.0
O A:HOH2071 3.4 42.2 1.0
CA A:ASN31 3.6 10.2 1.0
O A:HOH2078 3.6 19.7 1.0
C A:ASN31 3.8 12.7 1.0
CB A:VAL32 4.0 14.9 1.0
O A:VAL32 4.0 14.6 1.0
CA A:VAL32 4.0 10.5 1.0
O A:GLU30 4.1 13.1 1.0
NZ A:LYS314 4.2 23.6 0.8
CG2 A:VAL32 4.3 16.3 1.0
N A:ASN31 4.4 10.0 1.0
C A:VAL32 4.5 13.1 1.0
CE A:LYS314 4.5 21.7 0.8
OD1 A:ASN31 4.6 16.1 1.0
CB A:ASN31 4.6 11.6 1.0
C A:GLU30 4.6 10.6 1.0
CE A:LYS314 4.9 9.8 0.2
O A:ASN31 4.9 13.2 1.0
CG A:ASN31 5.0 13.7 1.0

Chlorine binding site 2 out of 2 in 1w5m

Go back to Chlorine Binding Sites List in 1w5m
Chlorine binding site 2 out of 2 in the Stepwise Introduction of Zinc Binding Site Into Porphobilinogen Synthase of Pseudomonas Aeruginosa (Mutations A129C and D139C)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Stepwise Introduction of Zinc Binding Site Into Porphobilinogen Synthase of Pseudomonas Aeruginosa (Mutations A129C and D139C) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1338

b:21.7
occ:0.80
O A:HOH2332 2.9 32.4 1.0
O A:HOH2328 2.9 21.9 1.0
N A:ASN196 3.1 11.2 1.0
O A:HOH2334 3.1 19.3 1.0
N A:THR195 3.6 12.5 0.7
C A:HIS194 3.6 12.6 1.0
N A:THR195 3.6 9.6 0.3
N A:VAL197 3.7 10.0 1.0
CA A:ASN196 3.7 11.8 1.0
CB A:ASN196 3.7 14.2 1.0
CA A:HIS194 3.7 13.3 1.0
O A:HOH2158 3.8 21.5 0.2
C A:ASN196 3.9 9.7 1.0
CG2 A:VAL197 4.0 12.0 1.0
O A:HIS194 4.1 11.2 1.0
C A:THR195 4.1 10.9 0.7
C A:THR195 4.2 13.7 0.3
CA A:THR195 4.3 12.1 0.7
CB A:HIS194 4.4 12.4 1.0
O A:GLY193 4.5 17.8 1.0
CA A:THR195 4.5 12.8 0.3
CG2 A:THR195 4.6 11.0 0.3
CA A:VAL197 4.7 9.3 1.0
CG A:ASN196 4.7 17.5 1.0
ND2 A:ASN196 4.7 16.9 1.0
O A:HOH2305 4.7 26.3 1.0
CB A:THR195 4.8 12.8 0.7
O A:HOH2313 4.8 19.1 1.0
O A:ASN196 4.8 11.3 1.0
CB A:VAL197 4.8 10.0 1.0
ND1 A:HIS194 4.8 17.4 1.0
N A:HIS194 5.0 12.7 1.0

Reference:

F.Frere, H.Reents, W.-D.Schubert, D.W.Heinz, D.Jahn. Tracking the Evolution of Porphobilinogen Synthase Metal Dependence in Vitro J.Mol.Biol. V. 345 1059 2005.
ISSN: ISSN 0022-2836
PubMed: 15644204
DOI: 10.1016/J.JMB.2004.10.053
Page generated: Thu Jul 10 20:12:31 2025

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