Chlorine in PDB 1z69: Crystal Structure of Methylenetetrahydromethanopterin Reductase (Mer) in Complex with Coenzyme F420

All present enzymatic activity of Crystal Structure of Methylenetetrahydromethanopterin Reductase (Mer) in Complex with Coenzyme F420:
1.5.99.11;

The structure of Crystal Structure of Methylenetetrahydromethanopterin Reductase (Mer) in Complex with Coenzyme F420, PDB code: 1z69 was solved by S.W.Aufhammer, E.Warkentin, U.Ermler, C.H.Hagemeier, R.K.Thauer, S.Shima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.95 / 2.61
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	81.810, 83.410, 99.170, 90.00, 91.15, 90.00
R / Rfree (%)	18.5 / 22.2

The binding sites of Chlorine atom in the Crystal Structure of Methylenetetrahydromethanopterin Reductase (Mer) in Complex with Coenzyme F420 (pdb code 1z69). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Methylenetetrahydromethanopterin Reductase (Mer) in Complex with Coenzyme F420, PDB code: 1z69:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Methylenetetrahydromethanopterin Reductase (Mer) in Complex with Coenzyme F420


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 Methylenetetrahydromethanopterin Reductase (Mer) in Complex with Coenzyme F420 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl4001 b:30.4 occ:1.00 O B:THR53 2.6 13.9 1.0 O C:THR53 2.7 15.7 1.0 O B:LEU51 3.1 19.7 1.0 O C:LEU51 3.1 25.0 1.0 O C:ALA50 3.2 16.7 1.0 ND2 B:ASN54 3.4 17.9 1.0 C C:LEU51 3.6 20.0 1.0 O B:ALA50 3.6 17.9 1.0 C B:LEU51 3.8 17.9 1.0 ND2 C:ASN54 3.8 12.2 1.0 C B:THR53 3.8 13.8 1.0 C C:THR53 3.9 14.4 1.0 CA C:LEU51 4.0 17.8 1.0 N B:THR53 4.1 11.3 1.0 N C:THR53 4.2 12.3 1.0 CG B:ASN54 4.3 17.6 1.0 C C:ALA50 4.3 17.9 1.0 CA B:LEU51 4.3 17.5 1.0 N C:ASN52 4.5 18.3 1.0 NH2 C:ARG87 4.5 3.8 1.0 CG C:ASN54 4.6 13.0 1.0 CA B:ASN54 4.6 15.3 1.0 N B:ASN52 4.6 15.6 1.0 N C:LEU51 4.7 17.6 1.0 CA B:THR53 4.7 12.1 1.0 N B:ASN54 4.7 14.8 1.0 CA C:ASN54 4.7 15.8 1.0 C B:ALA50 4.7 17.3 1.0 CA C:THR53 4.7 14.3 1.0 N C:ASN54 4.8 15.0 1.0 C B:ASN52 4.8 13.6 1.0 C C:ASN52 4.8 15.8 1.0 NH2 B:ARG87 4.9 8.5 1.0 CB B:ASN54 4.9 11.8 1.0 CA B:ASN52 4.9 12.9 1.0 CA C:ASN52 4.9 15.7 1.0 OD1 B:ASN54 4.9 16.1 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Methylenetetrahydromethanopterin Reductase (Mer) in Complex with Coenzyme F420


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Methylenetetrahydromethanopterin Reductase (Mer) in Complex with Coenzyme F420 within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl4002 b:25.9 occ:1.00 O D:THR53 2.6 16.4 1.0 O A:THR53 2.7 14.5 1.0 O A:LEU51 3.1 24.6 1.0 O D:LEU51 3.1 19.4 1.0 O D:ALA50 3.4 23.9 1.0 ND2 A:ASN54 3.5 16.9 1.0 ND2 D:ASN54 3.5 17.6 1.0 O A:ALA50 3.5 22.4 1.0 C D:LEU51 3.7 15.2 1.0 C A:LEU51 3.7 20.5 1.0 C D:THR53 3.8 15.5 1.0 C A:THR53 3.9 14.2 1.0 CA D:LEU51 4.1 16.4 1.0 N D:THR53 4.1 14.5 1.0 CA A:LEU51 4.2 20.5 1.0 N A:THR53 4.2 14.5 1.0 CG D:ASN54 4.3 14.3 1.0 CG A:ASN54 4.4 16.8 1.0 C D:ALA50 4.5 20.2 1.0 N D:ASN52 4.5 13.9 1.0 N A:ASN52 4.6 16.7 1.0 C A:ALA50 4.6 19.9 1.0 CA D:ASN54 4.6 16.4 1.0 CA D:THR53 4.7 15.6 1.0 CA A:ASN54 4.7 16.7 1.0 N D:ASN54 4.7 16.0 1.0 NH2 D:ARG87 4.7 5.8 1.0 CA A:THR53 4.7 13.5 1.0 C D:ASN52 4.7 15.0 1.0 NH2 A:ARG87 4.8 13.4 1.0 N A:ASN54 4.8 15.9 1.0 N D:LEU51 4.8 17.7 1.0 CA D:ASN52 4.9 14.2 1.0 C A:ASN52 4.9 16.7 1.0 N A:LEU51 4.9 20.3 1.0 CA A:ASN52 4.9 16.0 1.0 CB D:ASN54 5.0 12.5 1.0 OD1 D:ASN54 5.0 12.8 1.0

S.W.Aufhammer, E.Warkentin, U.Ermler, C.H.Hagemeier, R.K.Thauer, S.Shima. Crystal Structure of Methylenetetrahydromethanopterin Reductase (Mer) in Complex with Coenzyme F420: Architecture of the F420/Fmn Binding Site of Enzymes Within the Nonprolyl Cis-Peptide Containing Bacterial Luciferase Family Protein Sci. V. 14 1840 2005.
ISSN: ISSN 0961-8368
PubMed: 15937276
DOI: 10.1110/PS.041289805