Chlorine in PDB 9mya: Crystal Structure of Unliganded Retro-Aldolase RA95 (277 K)

The structure of Crystal Structure of Unliganded Retro-Aldolase RA95 (277 K), PDB code: 9mya was solved by R.A.Chica, S.E.Hunt, M.C.Thompson, A.Martinez, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.00 / 1.89
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	97.992, 65.152, 44.377, 90, 90, 90
R / Rfree (%)	16 / 20

The binding sites of Chlorine atom in the Crystal Structure of Unliganded Retro-Aldolase RA95 (277 K) (pdb code 9mya). 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 Unliganded Retro-Aldolase RA95 (277 K), PDB code: 9mya:

Chlorine binding site 1 out of 1 in the Crystal Structure of Unliganded Retro-Aldolase RA95 (277 K)


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 Unliganded Retro-Aldolase RA95 (277 K) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:30.3 occ:1.00 H A:SER181 2.5 27.6 1.0 H A:ARG182 2.7 29.8 1.0 HD3 A:LYS210 2.7 24.9 0.3 HB3 A:MET180 2.9 27.0 1.0 HZ1 A:LYS210 3.0 31.3 0.3 HD3 A:LYS210 3.0 26.0 0.7 HG A:SER181 3.0 30.6 1.0 HA A:MET180 3.2 22.5 1.0 N A:SER181 3.2 23.0 1.0 HG3 A:ARG182 3.4 63.9 1.0 N A:ARG182 3.4 24.8 1.0 HE3 A:LYS210 3.4 34.3 0.7 HB3 A:LYS210 3.5 18.7 0.3 HB2 A:ARG182 3.5 45.8 1.0 HE2 A:MET180 3.5 53.7 1.0 HE3 A:MET180 3.5 53.7 1.0 HB3 A:LYS210 3.5 18.7 0.7 HG2 A:LYS210 3.5 25.7 0.3 HG2 A:LYS210 3.5 25.8 0.7 CD A:LYS210 3.6 20.7 0.3 CB A:MET180 3.6 22.5 1.0 OG A:SER181 3.7 25.6 1.0 CD A:LYS210 3.7 21.6 0.7 CA A:MET180 3.7 18.7 1.0 HG2 A:MET180 3.8 28.8 1.0 HD2 A:ARG182 3.8 73.9 1.0 NZ A:LYS210 3.8 26.1 0.3 CG A:LYS210 3.9 21.4 0.3 CE A:MET180 4.0 44.8 1.0 C A:MET180 4.0 27.6 1.0 CG A:LYS210 4.0 21.5 0.7 CE A:LYS210 4.0 28.6 0.7 CB A:ARG182 4.1 38.2 1.0 CG A:ARG182 4.1 53.3 1.0 CE A:LYS210 4.1 27.8 0.3 O A:LYS210 4.1 17.5 0.7 CA A:SER181 4.1 20.9 1.0 O A:LYS210 4.1 17.5 0.3 HZ2 A:LYS210 4.1 31.3 0.3 CB A:LYS210 4.2 15.6 0.3 HE3 A:LYS210 4.2 33.3 0.3 C A:SER181 4.2 26.9 1.0 CB A:LYS210 4.2 15.6 0.7 CG A:MET180 4.2 24.0 1.0 CA A:ARG182 4.3 36.0 1.0 HD2 A:LYS210 4.3 24.9 0.3 HE2 A:LYS210 4.4 34.3 0.7 HZ3 A:LYS210 4.4 31.3 0.3 HB2 A:MET180 4.4 27.0 1.0 CD A:ARG182 4.4 61.6 1.0 O A:ARG182 4.5 39.5 1.0 CB A:SER181 4.5 30.2 1.0 HD2 A:LYS210 4.6 26.0 0.7 C A:LYS210 4.6 17.5 0.3 C A:LYS210 4.6 17.4 0.7 HE1 A:MET180 4.7 53.7 1.0 C A:ARG182 4.8 39.2 1.0 HG3 A:LYS210 4.8 25.7 0.3 HB2 A:LYS210 4.8 18.7 0.3 HB3 A:SER181 4.9 36.2 1.0 HB2 A:LYS210 4.9 18.7 0.7 HG3 A:LYS210 4.9 25.8 0.7 HG2 A:ARG182 4.9 63.9 1.0 HB3 A:ARG182 5.0 45.8 1.0 HA A:SER181 5.0 25.1 1.0 SD A:MET180 5.0 29.0 1.0

S.E.Hunt, A.Martinez, M.C.Thompson, R.A.Chica. Distal Mutations in A Designed Retro-Aldolase Alter Loop Dynamics to Shift and Accelerate the Rate-Limiting Step To Be Published.