Chlorine in PDB 5wly: E. Coli Lpxh- 8 Mutations

All present enzymatic activity of E. Coli Lpxh- 8 Mutations:
3.6.1.54;

The structure of E. Coli Lpxh- 8 Mutations, PDB code: 5wly was solved by T.E.Bohl, H.Aihara, K.Shi, J.K.Lee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.23 / 2.00
Space group	P 21 2 21
Cell size a, b, c (Å), α, β, γ (°)	57.012, 62.064, 66.047, 90.00, 90.00, 90.00
R / Rfree (%)	19.8 / 22.7

The structure of E. Coli Lpxh- 8 Mutations also contains other interesting chemical elements:

Manganese

(Mn)

2 atoms

The binding sites of Chlorine atom in the E. Coli Lpxh- 8 Mutations (pdb code 5wly). 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 E. Coli Lpxh- 8 Mutations, PDB code: 5wly:

Chlorine binding site 1 out of 1 in the E. Coli Lpxh- 8 Mutations


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of E. Coli Lpxh- 8 Mutations within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl303 b:27.6 occ:0.83 HH11 A:ARG155 2.3 41.0 1.0 HD22 A:ASN79 2.3 36.5 1.0 HH11 A:ARG80 2.5 38.9 1.0 O A:HOH429 2.9 25.3 1.0 NH1 A:ARG155 3.1 33.6 1.0 ND2 A:ASN79 3.1 29.8 1.0 NH1 A:ARG80 3.2 31.8 1.0 HD2 A:ARG155 3.2 39.5 1.0 HD2 A:ARG80 3.2 36.1 1.0 HD3 A:ARG155 3.3 39.5 1.0 HH12 A:ARG155 3.4 41.0 1.0 HH12 A:ARG80 3.4 38.9 1.0 HD21 A:ASN79 3.5 36.5 1.0 HB2 A:ASN79 3.5 34.9 1.0 CD A:ARG155 3.7 32.3 1.0 HD3 A:ARG80 3.8 36.1 1.0 CD A:ARG80 3.9 29.5 1.0 O A:ASN79 4.1 21.9 1.0 CZ A:ARG155 4.2 33.6 1.0 CG A:ASN79 4.2 30.6 1.0 CB A:ASN79 4.3 28.5 1.0 CZ A:ARG80 4.3 30.3 1.0 NE A:ARG155 4.4 33.3 1.0 HA A:ARG80 4.5 33.0 1.0 NE A:ARG80 4.5 29.2 1.0 C A:ASN79 4.5 22.9 1.0 O A:HOH452 4.8 27.1 1.0 HB3 A:ASN79 4.9 34.9 1.0 CG A:ARG155 4.9 31.9 1.0 HB2 A:ARG155 5.0 40.5 1.0 HG2 A:ARG155 5.0 38.9 1.0

T.E.Bohl, P.Ieong, J.K.Lee, T.Lee, J.Kankanala, K.Shi, O.Demir, K.Kurahashi, R.E.Amaro, Z.Wang, H.Aihara. The Substrate-Binding Cap of the Udp-Diacylglucosamine Pyrophosphatase Lpxh Is Highly Flexible, Enabling Facile Substrate Binding and Product Release. J. Biol. Chem. V. 293 7969 2018.
ISSN: ESSN 1083-351X
PubMed: 29626094
DOI: 10.1074/JBC.RA118.002503