Chlorine in PDB 6rnv: The Crystal Structure of Thermosynechococcus Elongatus Protochlorophyllide Oxidoreductase (Por)

The structure of The Crystal Structure of Thermosynechococcus Elongatus Protochlorophyllide Oxidoreductase (Por), PDB code: 6rnv was solved by C.W.Levy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	53.08 / 1.27
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	66.847, 66.847, 133.008, 90.00, 90.00, 120.00
R / Rfree (%)	15.3 / 18.6

The binding sites of Chlorine atom in the The Crystal Structure of Thermosynechococcus Elongatus Protochlorophyllide Oxidoreductase (Por) (pdb code 6rnv). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the The Crystal Structure of Thermosynechococcus Elongatus Protochlorophyllide Oxidoreductase (Por), PDB code: 6rnv:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the The Crystal Structure of Thermosynechococcus Elongatus Protochlorophyllide Oxidoreductase (Por)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of The Crystal Structure of Thermosynechococcus Elongatus Protochlorophyllide Oxidoreductase (Por) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl401 b:17.0 occ:1.00 H A:LYS99 2.4 18.2 1.0 H A:GLU100 2.5 18.4 1.0 O A:HOH675 3.1 29.3 1.0 HA A:LEU98 3.1 17.7 1.0 N A:LYS99 3.2 15.2 1.0 HD22 A:LEU98 3.3 19.6 1.0 HB2 A:GLU100 3.3 21.0 1.0 N A:GLU100 3.4 15.3 1.0 HB2 A:LYS99 3.5 22.0 1.0 HD23 A:LEU98 3.7 19.6 1.0 CA A:LEU98 3.9 14.7 1.0 O A:GLU100 3.9 13.5 1.0 HB3 A:LEU98 3.9 17.3 1.0 CD2 A:LEU98 3.9 16.3 1.0 CA A:LYS99 4.0 17.2 1.0 HG2 A:GLU100 4.0 27.9 1.0 C A:LEU98 4.0 15.3 1.0 CB A:GLU100 4.1 17.5 1.0 C A:LYS99 4.1 16.5 1.0 CA A:GLU100 4.2 15.3 1.0 CB A:LYS99 4.2 18.4 1.0 CB A:LEU98 4.4 14.4 1.0 C A:GLU100 4.5 13.3 1.0 CG A:GLU100 4.5 23.3 1.0 HG3 A:LYS99 4.5 27.9 1.0 HE2 A:LYS99 4.6 42.2 1.0 HD21 A:LEU98 4.7 19.6 1.0 HG3 A:GLU100 4.7 27.9 1.0 O A:LEU97 4.8 19.1 1.0 CG A:LEU98 4.8 15.4 1.0 HB3 A:GLU100 4.9 21.0 1.0 HA A:LYS99 4.9 20.6 1.0 HB3 A:LYS99 5.0 22.0 1.0 CG A:LYS99 5.0 23.3 1.0

Chlorine binding site 2 out of 2 in the The Crystal Structure of Thermosynechococcus Elongatus Protochlorophyllide Oxidoreductase (Por)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of The Crystal Structure of Thermosynechococcus Elongatus Protochlorophyllide Oxidoreductase (Por) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl402 b:25.3 occ:1.00 H A:LEU97 2.4 19.8 1.0 HA A:TYR95 2.9 19.4 0.5 HB2 A:LEU97 2.9 25.0 1.0 HA A:TYR95 3.0 19.4 0.5 HD2 A:PRO96 3.1 25.4 1.0 HB3 A:TYR95 3.1 21.5 0.5 HD1 A:TYR95 3.2 21.5 0.5 N A:LEU97 3.2 16.5 1.0 C A:TYR95 3.3 17.4 0.5 HB3 A:TYR95 3.4 20.2 0.5 C A:TYR95 3.4 17.6 0.5 HG A:LEU98 3.4 18.5 1.0 CA A:TYR95 3.5 16.1 0.5 H A:LEU98 3.5 18.2 1.0 CA A:TYR95 3.5 16.1 0.5 N A:PRO96 3.5 19.4 1.0 CB A:LEU97 3.7 20.9 1.0 HG A:LEU97 3.7 31.3 1.0 CD A:PRO96 3.7 21.1 1.0 O A:TYR95 3.7 18.2 0.5 CB A:TYR95 3.8 17.9 0.5 HG2 A:PRO96 3.8 27.9 1.0 HD2 A:TYR95 3.8 24.1 0.5 CA A:LEU97 3.8 17.4 1.0 CB A:TYR95 3.9 16.8 0.5 O A:TYR95 3.9 19.0 0.5 CD1 A:TYR95 3.9 17.9 0.5 N A:LEU98 4.0 15.2 1.0 HD12 A:LEU97 4.1 34.9 1.0 CG A:LEU97 4.1 26.1 1.0 C A:LEU97 4.2 17.5 1.0 C A:PRO96 4.2 19.0 1.0 CG A:PRO96 4.3 23.2 1.0 CG A:TYR95 4.3 17.6 0.5 HD23 A:LEU98 4.4 19.6 1.0 CG A:LEU98 4.4 15.4 1.0 CA A:PRO96 4.4 20.8 1.0 HB3 A:LEU97 4.5 25.0 1.0 HB2 A:TYR95 4.5 21.5 0.5 HD3 A:PRO96 4.5 25.4 1.0 CD2 A:TYR95 4.6 20.1 0.5 CD1 A:LEU97 4.7 29.1 1.0 CG A:TYR95 4.7 19.3 0.5 HA A:LEU97 4.7 20.9 1.0 HB2 A:TYR95 4.8 20.2 0.5 CD2 A:LEU98 4.8 16.3 1.0 HD21 A:LEU98 4.8 19.6 1.0 N A:TYR95 4.9 15.6 0.5 N A:TYR95 4.9 15.5 0.5 CA A:LEU98 5.0 14.7 1.0 CE1 A:TYR95 5.0 18.5 0.5

S.Zhang, D.J.Heyes, L.Feng, W.Sun, L.O.Johannissen, H.Liu, C.W.Levy, X.Li, J.Yang, X.Yu, M.Lin, S.J.O.Hardman, R.Hoeven, M.Sakuma, S.Hay, D.Leys, Z.Rao, A.Zhou, Q.Cheng, N.S.Scrutton. Structural Basis For Enzymatic Photocatalysis in Chlorophyll Biosynthesis. Nature V. 574 722 2019.
ISSN: ESSN 1476-4687
PubMed: 31645759
DOI: 10.1038/S41586-019-1685-2