Manganese in PDB 4m0x: Crystal Structure of 2-Chloromuconate Cycloisomerase From Rhodococcus Opacus 1CP

The structure of Crystal Structure of 2-Chloromuconate Cycloisomerase From Rhodococcus Opacus 1CP, PDB code: 4m0x was solved by M.Ferraroni, M.Kolomytseva, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.70
Space group	P 4 21 2
Cell size a, b, c (Å), α, β, γ (°)	121.110, 121.110, 110.560, 90.00, 90.00, 90.00
R / Rfree (%)	17.7 / 26.5

The structure of Crystal Structure of 2-Chloromuconate Cycloisomerase From Rhodococcus Opacus 1CP also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Manganese atom in the Crystal Structure of 2-Chloromuconate Cycloisomerase From Rhodococcus Opacus 1CP (pdb code 4m0x). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of 2-Chloromuconate Cycloisomerase From Rhodococcus Opacus 1CP, PDB code: 4m0x:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of 2-Chloromuconate Cycloisomerase From Rhodococcus Opacus 1CP


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of 2-Chloromuconate Cycloisomerase From Rhodococcus Opacus 1CP within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn401 b:27.3 occ:1.00 OD2 A:ASP196 2.1 28.2 1.0 OE2 A:GLU222 2.2 24.6 1.0 O A:HOH562 2.2 15.9 1.0 OD2 A:ASP247 2.2 21.2 1.0 O A:HOH605 2.5 30.0 1.0 O A:HOH606 2.7 57.6 1.0 CL A:CL402 2.8 46.5 1.0 CD A:GLU222 3.0 26.7 1.0 CG A:ASP196 3.2 26.7 1.0 CG A:ASP247 3.3 22.5 1.0 OE1 A:GLU222 3.5 28.1 1.0 OD1 A:ASP196 3.6 26.6 1.0 CB A:ASP247 3.8 21.3 1.0 NZ A:LYS165 3.9 28.2 1.0 NZ A:LYS271 4.1 20.6 1.0 CG A:GLU222 4.1 26.2 1.0 OD1 A:ASN198 4.2 38.5 1.0 OE1 A:GLU248 4.2 30.0 1.0 NZ A:LYS167 4.3 51.7 1.0 OD1 A:ASP247 4.4 23.1 1.0 CB A:ASP196 4.5 24.8 1.0 CE A:LYS165 4.6 26.1 1.0 OE2 A:GLU248 4.7 30.6 1.0 NE1 A:TRP58 4.8 25.0 1.0 CD A:GLU248 4.8 28.6 1.0 CE A:LYS167 5.0 57.2 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of 2-Chloromuconate Cycloisomerase From Rhodococcus Opacus 1CP


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of 2-Chloromuconate Cycloisomerase From Rhodococcus Opacus 1CP within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn401 b:39.9 occ:1.00 OE2 B:GLU222 1.8 33.8 1.0 OD2 B:ASP196 2.2 48.6 1.0 OD2 B:ASP247 2.3 34.1 1.0 O B:HOH564 2.7 32.3 1.0 CD B:GLU222 2.9 34.5 1.0 CG B:ASP196 3.0 44.6 1.0 OD1 B:ASP196 3.0 44.2 1.0 CG B:ASP247 3.4 33.5 1.0 NZ B:LYS167 3.7 65.2 1.0 OD1 B:ASN198 3.7 43.8 1.0 OE1 B:GLU222 3.7 33.5 1.0 CB B:ASP247 3.7 31.9 1.0 CG B:GLU222 3.8 33.6 1.0 OE1 B:GLU248 3.8 51.1 1.0 NZ B:LYS271 4.0 35.9 1.0 OE2 B:GLU248 4.0 46.8 1.0 NZ B:LYS165 4.1 32.3 1.0 CD B:GLU248 4.3 45.4 1.0 CB B:ASP196 4.4 40.8 1.0 OD1 B:ASP247 4.5 36.7 1.0 NE1 B:TRP58 4.5 40.5 1.0 CG B:ASN198 4.8 38.0 1.0 CE B:LYS167 4.9 63.3 1.0 CB B:GLU222 4.9 30.2 1.0 CZ2 B:TRP58 4.9 37.5 1.0 CE B:LYS165 5.0 35.5 1.0

M.Kolomytseva, M.Ferraroni, A.Chernykh, L.Golovleva, A.Scozzafava. Structural Basis For the Substrate Specificity and the Absence of Dehalogenation Activity in 2-Chloromuconate Cycloisomerase From Rhodococcus Opacus 1CP. Biochim.Biophys.Acta V.1844 1541 2014.
ISSN: ISSN 0006-3002
PubMed: 24768773
DOI: 10.1016/J.BBAPAP.2014.04.008