Chlorine in PDB 9q8f: Structure of the (6-4) Photolyase of Caulobacter Crescentus with K48A Mutation in Its Dark Adapted and Oxidized State Determined By Synchrotron

The structure of Structure of the (6-4) Photolyase of Caulobacter Crescentus with K48A Mutation in Its Dark Adapted and Oxidized State Determined By Synchrotron, PDB code: 9q8f was solved by W.Po Hsun, M.Maestre-Reyna, L.-O.Essen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.96 / 1.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	48.984, 102.102, 102.944, 90, 90, 90
R / Rfree (%)	13.8 / 16.5

The structure of Structure of the (6-4) Photolyase of Caulobacter Crescentus with K48A Mutation in Its Dark Adapted and Oxidized State Determined By Synchrotron also contains other interesting chemical elements:

Iron	(Fe)	4 atoms
Magnesium	(Mg)	1 atom

The binding sites of Chlorine atom in the Structure of the (6-4) Photolyase of Caulobacter Crescentus with K48A Mutation in Its Dark Adapted and Oxidized State Determined By Synchrotron (pdb code 9q8f). 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 Structure of the (6-4) Photolyase of Caulobacter Crescentus with K48A Mutation in Its Dark Adapted and Oxidized State Determined By Synchrotron, PDB code: 9q8f:

Chlorine binding site 1 out of 1 in the Structure of the (6-4) Photolyase of Caulobacter Crescentus with K48A Mutation in Its Dark Adapted and Oxidized State Determined By Synchrotron


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of the (6-4) Photolyase of Caulobacter Crescentus with K48A Mutation in Its Dark Adapted and Oxidized State Determined By Synchrotron within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl610 b:11.8 occ:0.73 H A:GLU399 2.3 11.6 1.0 HO3 A:GOL609 2.5 27.8 0.6 HA A:TYR398 2.8 10.5 1.0 HD3 A:LYS107 2.8 21.0 0.4 O3' A:DLZ602 3.0 20.8 0.5 HD2 A:LYS107 3.0 22.7 0.6 HB2 A:LYS107 3.0 15.9 0.4 HB2 A:LYS107 3.0 18.3 0.6 N A:GLU399 3.1 9.7 1.0 O A:HOH902 3.2 18.4 1.0 O3 A:GOL609 3.2 23.1 0.6 O A:HOH709 3.3 34.3 1.0 HE1 A:MET391 3.4 13.5 1.0 HB2 A:GLU399 3.4 14.2 1.0 HZ3 A:TRP42 3.5 22.0 1.0 H5' A:DLZ602 3.5 24.5 0.5 HD1 A:TYR398 3.5 11.4 1.0 HB3 A:TYR398 3.6 12.2 1.0 CA A:TYR398 3.6 8.8 1.0 HE2 A:LYS107 3.7 13.0 0.4 HE2 A:MET391 3.7 13.5 1.0 CD A:LYS107 3.7 17.5 0.4 CD A:LYS107 3.7 18.9 0.6 HD3 A:LYS107 3.8 22.7 0.6 C A:TYR398 3.9 8.8 1.0 H3' A:DLZ602 3.9 25.1 0.5 CB A:LYS107 3.9 13.3 0.4 CB A:LYS107 3.9 15.3 0.6 CE A:MET391 4.0 11.2 1.0 H5'A A:DLZ602 4.0 24.5 0.5 CB A:GLU399 4.0 11.8 1.0 C3' A:DLZ602 4.0 20.9 0.5 HB3 A:GLU399 4.1 14.2 1.0 CB A:TYR398 4.1 10.2 1.0 HG3 A:LYS107 4.1 21.6 0.6 CE A:LYS107 4.1 10.8 0.4 CA A:GLU399 4.1 8.8 1.0 O A:HOH710 4.2 36.6 0.5 CG A:LYS107 4.2 18.0 0.6 C5' A:DLZ602 4.2 20.4 0.5 HZ2 A:LYS107 4.2 14.1 0.4 CZ3 A:TRP42 4.2 18.3 1.0 CG A:LYS107 4.2 17.0 0.4 CD1 A:TYR398 4.3 9.5 1.0 HG3 A:LYS107 4.3 20.4 0.4 C3 A:GOL609 4.3 22.9 0.6 HB3 A:LYS107 4.4 15.9 0.4 HB3 A:LYS107 4.4 18.3 0.6 H32 A:GOL609 4.4 27.5 0.6 HD2 A:LYS107 4.4 21.0 0.4 HO3 A:GOL608 4.5 29.3 0.6 NZ A:LYS107 4.6 11.8 0.4 O A:GLY106 4.6 11.9 1.0 HA A:GLU399 4.6 10.6 1.0 HZ1 A:LYS107 4.6 14.1 0.4 HH2 A:TRP42 4.6 20.7 1.0 CG A:TYR398 4.7 9.7 1.0 HE3 A:MET391 4.7 13.5 1.0 C1 A:GOL609 4.8 22.1 0.6 C4' A:DLZ602 4.8 20.7 0.5 HA A:LYS107 4.8 13.9 0.4 C2 A:GOL609 4.8 22.5 0.6 HA A:LYS107 4.8 13.8 0.6 CH2 A:TRP42 4.8 17.2 1.0 H7A A:DLZ602 4.8 24.7 0.5 N A:TYR398 4.9 7.2 1.0 H A:TRP400 4.9 9.9 1.0 HO2' A:DLZ602 4.9 25.5 0.5 HZ3 A:LYS107 4.9 33.8 0.6 CA A:LYS107 4.9 11.6 0.4 CA A:LYS107 4.9 11.5 0.6 HB2 A:TYR398 4.9 12.2 1.0 O A:ALA397 4.9 9.1 1.0 O3 A:GOL608 5.0 24.4 0.6

P.H.Wang, Y.Hosokawa, J.C Soares, H.J.Emmerich, V.Fuchs, N.Caramello, S.Engilberge, A.Bologna, C.J.Rosner, M.Nakamura, M.Watad, F.Luo, S.Owada, T.Tosha, J.Kang, K.Tono, Y.Bessho, E.Nango, A.J.Pierik, A.Royant, M.D.Tsai, J.Yamamoto, M.Maestre-Reyna, L.O.Essen. Redox-State-Dependent Structural Changes Within A Prokaryotic 6-4 Photolyase. J.Am.Chem.Soc. 2025.
ISSN: ESSN 1520-5126
PubMed: 40298610
DOI: 10.1021/JACS.4C18116