Chlorine in PDB 5xu7: Crystal Structure of Escherichia Coli Holo-[Acyl-Carrier-Protein] Synthase (Acps)

All present enzymatic activity of Crystal Structure of Escherichia Coli Holo-[Acyl-Carrier-Protein] Synthase (Acps):
2.7.8.7;

The structure of Crystal Structure of Escherichia Coli Holo-[Acyl-Carrier-Protein] Synthase (Acps), PDB code: 5xu7 was solved by Y.P.Liao, D.L.Wang, D.P.Yin, Q.Y.Zhang, Y.M.Wang, D.Q.Wang, H.X.Zhu, S.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.84
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	97.620, 97.620, 96.140, 90.00, 90.00, 90.00
R / Rfree (%)	17.5 / 21.4

The binding sites of Chlorine atom in the Crystal Structure of Escherichia Coli Holo-[Acyl-Carrier-Protein] Synthase (Acps) (pdb code 5xu7). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystal Structure of Escherichia Coli Holo-[Acyl-Carrier-Protein] Synthase (Acps), PDB code: 5xu7:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Crystal Structure of Escherichia Coli Holo-[Acyl-Carrier-Protein] Synthase (Acps)


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 Escherichia Coli Holo-[Acyl-Carrier-Protein] Synthase (Acps) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl201 b:27.1 occ:1.00 C A:GLN45 3.3 20.3 1.0 N A:VAL47 3.3 18.8 1.0 CA A:GLN45 3.5 22.8 1.0 N A:ARG48 3.5 17.0 1.0 O A:HOH361 3.5 41.4 1.0 N A:PRO46 3.6 21.1 1.0 CB A:VAL47 3.6 20.2 1.0 O A:GLN45 3.7 19.1 1.0 CB A:GLN45 3.7 24.6 1.0 CA A:VAL47 3.9 18.5 1.0 CD A:PRO46 3.9 22.6 1.0 CG2 A:VAL47 4.1 23.0 1.0 C A:VAL47 4.2 17.1 1.0 CB A:ARG48 4.2 18.7 1.0 C A:PRO46 4.3 18.8 1.0 CG A:GLN45 4.3 27.7 1.0 CA A:ARG48 4.5 17.3 1.0 CA A:PRO46 4.5 20.4 1.0 CG A:PRO46 4.7 22.3 1.0 O A:HOH378 4.7 38.3 1.0 CG1 A:VAL47 4.8 20.1 1.0 N A:GLN45 4.9 22.7 1.0

Chlorine binding site 2 out of 3 in the Crystal Structure of Escherichia Coli Holo-[Acyl-Carrier-Protein] Synthase (Acps)


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 Escherichia Coli Holo-[Acyl-Carrier-Protein] Synthase (Acps) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl202 b:36.8 occ:1.00 O A:HOH384 2.9 32.1 1.0 O A:HOH320 3.1 22.9 1.0 N A:PHE74 3.2 25.4 1.0 O A:HOH409 3.3 35.4 1.0 O A:HOH380 3.4 44.9 1.0 O A:HOH353 3.4 42.9 1.0 CB A:PHE74 3.7 23.4 1.0 CG A:PHE74 3.9 24.5 1.0 CA A:ALA73 3.9 30.8 1.0 NE A:ARG30 3.9 25.2 1.0 C A:ALA73 4.0 27.0 1.0 CA A:PHE74 4.0 23.7 1.0 CD1 A:PHE74 4.3 25.4 1.0 NH2 A:ARG30 4.3 25.7 1.0 CG A:ARG30 4.3 24.2 1.0 CZ A:ARG30 4.4 26.5 1.0 CD2 A:PHE74 4.4 25.8 1.0 CG1 A:VAL31 4.4 20.5 1.0 CB A:ALA73 4.5 31.8 1.0 CD A:ARG30 4.7 25.0 1.0 O A:LEU72 4.7 39.2 1.0 O A:ARG30 4.8 22.6 1.0 N A:ASN75 4.9 23.5 1.0 CE1 A:PHE74 5.0 26.0 1.0

Chlorine binding site 3 out of 3 in the Crystal Structure of Escherichia Coli Holo-[Acyl-Carrier-Protein] Synthase (Acps)


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 Escherichia Coli Holo-[Acyl-Carrier-Protein] Synthase (Acps) within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl201 b:43.6 occ:1.00 N C:VAL47 3.3 25.5 1.0 C C:GLN45 3.3 33.1 1.0 CA C:GLN45 3.4 38.6 1.0 CB C:VAL47 3.4 25.9 1.0 CB C:GLN45 3.4 40.9 1.0 N C:ARG48 3.7 21.4 1.0 N C:PRO46 3.7 31.3 1.0 O C:GLN45 3.7 29.7 1.0 CG2 C:VAL47 3.8 28.6 1.0 CA C:VAL47 3.8 24.2 1.0 CD C:PRO46 4.0 33.5 1.0 CG C:GLN45 4.0 46.4 1.0 C C:VAL47 4.3 22.0 1.0 C C:PRO46 4.3 27.4 1.0 CB C:ARG48 4.5 22.2 1.0 CA C:PRO46 4.5 30.9 1.0 CG C:PRO46 4.7 34.5 1.0 CG1 C:VAL47 4.7 25.6 1.0 CA C:ARG48 4.7 20.9 1.0 CD C:GLN45 4.7 50.9 1.0 N C:GLN45 4.8 41.3 1.0 OE1 C:GLN45 5.0 55.1 1.0

Y.P.Liao, D.L.Wang, D.P.Yin, Q.Y.Zhang, Y.M.Wang, D.Q.Wang, H.X.Zhu, S.Chen. Crystal Structures of Acyl Carrier Protein Synthases (Acps) From Three Gram-Negative Bacteria To Be Published.