Chlorine in PDB 4tku: Reactivated Nitrogenase Mofe-Protein From A. Vinelandii

All present enzymatic activity of Reactivated Nitrogenase Mofe-Protein From A. Vinelandii:
1.18.6.1;

The structure of Reactivated Nitrogenase Mofe-Protein From A. Vinelandii, PDB code: 4tku was solved by T.Spatzal, K.Perez, O.Einsle, J.B.Howard, D.C.Rees, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.65 / 1.43
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	80.941, 130.785, 107.005, 90.00, 110.58, 90.00
R / Rfree (%)	13.2 / 14.2

The structure of Reactivated Nitrogenase Mofe-Protein From A. Vinelandii also contains other interesting chemical elements:

Molybdenum	(Mo)	2 atoms
Iron	(Fe)	32 atoms

The binding sites of Chlorine atom in the Reactivated Nitrogenase Mofe-Protein From A. Vinelandii (pdb code 4tku). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Reactivated Nitrogenase Mofe-Protein From A. Vinelandii, PDB code: 4tku:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Reactivated Nitrogenase Mofe-Protein From A. Vinelandii


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Reactivated Nitrogenase Mofe-Protein From A. Vinelandii within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl504 b:11.1 occ:0.70 O B:HOH728 2.9 9.6 1.0 OG1 A:THR111 3.0 9.5 1.0 NH2 A:ARG93 3.3 9.0 1.0 CG B:PHE450 3.4 9.2 1.0 CB B:PHE450 3.6 7.8 1.0 NH1 B:ARG453 3.7 16.0 0.7 O A:THR111 3.7 9.2 1.0 CG2 A:THR104 3.7 8.8 1.0 C A:THR111 3.8 7.8 1.0 CD2 B:PHE450 3.8 9.7 1.0 NH2 B:ARG453 3.8 18.1 0.8 CD1 B:PHE450 3.8 10.3 1.0 CB A:THR111 3.8 8.7 1.0 CG A:MET112 3.9 10.2 1.0 NH2 B:ARG453 4.0 18.5 0.2 N A:MET112 4.1 8.1 1.0 CZ B:ARG453 4.2 14.6 0.7 CE2 B:PHE450 4.3 11.9 1.0 CE1 B:PHE450 4.3 12.1 1.0 CA A:THR111 4.4 7.5 1.0 CA A:MET112 4.4 8.0 1.0 CZ A:ARG93 4.5 9.1 1.0 CZ B:PHE450 4.6 10.9 1.0 O B:HOH947 4.7 15.9 1.0 O A:HOH861 4.7 25.1 1.0 CB A:MET112 4.8 8.8 1.0 NE A:ARG93 4.8 7.8 1.0 CB A:THR104 4.9 8.6 1.0 ND2 B:ASN65 5.0 7.6 1.0

Chlorine binding site 2 out of 2 in the Reactivated Nitrogenase Mofe-Protein From A. Vinelandii


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Reactivated Nitrogenase Mofe-Protein From A. Vinelandii within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl504 b:10.5 occ:0.70 O D:HOH716 2.9 10.3 1.0 OG1 C:THR111 2.9 9.1 1.0 NH2 C:ARG93 3.3 8.7 1.0 CG D:PHE450 3.4 8.9 1.0 CB D:PHE450 3.6 8.0 1.0 NH1 D:ARG453 3.6 18.4 0.8 O C:THR111 3.7 8.9 1.0 NH2 D:ARG453 3.7 14.6 0.8 CD2 D:PHE450 3.7 9.3 1.0 CG2 C:THR104 3.7 9.8 1.0 C C:THR111 3.8 7.6 1.0 CB C:THR111 3.8 8.9 1.0 CD1 D:PHE450 3.8 9.8 1.0 CG C:MET112 3.9 9.8 1.0 NH1 D:ARG453 3.9 16.0 0.2 N C:MET112 4.1 8.6 1.0 CZ D:ARG453 4.1 15.3 0.8 CE2 D:PHE450 4.3 11.7 1.0 CA C:THR111 4.4 7.6 1.0 CE1 D:PHE450 4.4 11.8 1.0 CA C:MET112 4.4 8.2 1.0 CZ C:ARG93 4.5 8.4 1.0 CZ D:PHE450 4.6 12.8 1.0 O C:HOH871 4.6 30.1 1.0 O D:HOH889 4.7 16.6 1.0 CB C:MET112 4.8 9.0 1.0 NE C:ARG93 4.8 7.4 1.0 CB C:THR104 4.9 9.5 1.0 N C:THR111 5.0 8.1 1.0

T.Spatzal, K.A.Perez, O.Einsle, J.B.Howard, D.C.Rees. Ligand Binding to the Femo-Cofactor: Structures of Co-Bound and Reactivated Nitrogenase. Science V. 345 1620 2014.
ISSN: ESSN 1095-9203
PubMed: 25258081
DOI: 10.1126/SCIENCE.1256679