Manganese in PDB 1muc: Structure of Muconate Lactonizing Enzyme at 1.85 Angstroms Resolution

All present enzymatic activity of Structure of Muconate Lactonizing Enzyme at 1.85 Angstroms Resolution:
5.5.1.1;

The structure of Structure of Muconate Lactonizing Enzyme at 1.85 Angstroms Resolution, PDB code: 1muc was solved by S.Helin, P.C.Kahn, B.H.L.Guha, D.J.Mallows, A.Goldman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 1.85
Space group	I 4
Cell size a, b, c (Å), α, β, γ (°)	139.300, 139.300, 84.100, 90.00, 90.00, 90.00
R / Rfree (%)	16.8 / n/a

The binding sites of Manganese atom in the Structure of Muconate Lactonizing Enzyme at 1.85 Angstroms Resolution (pdb code 1muc). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Structure of Muconate Lactonizing Enzyme at 1.85 Angstroms Resolution, PDB code: 1muc:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Structure of Muconate Lactonizing Enzyme at 1.85 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of Muconate Lactonizing Enzyme at 1.85 Angstroms Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn374 b:15.6 occ:1.00 O A:HOH444 1.7 30.8 1.0 O A:HOH390 2.1 10.8 1.0 OE2 A:GLU224 2.1 11.6 1.0 OD2 A:ASP249 2.2 18.0 1.0 O A:HOH408 2.2 13.7 1.0 OD2 A:ASP198 2.3 13.8 1.0 CD A:GLU224 3.0 5.1 1.0 CG A:ASP198 3.2 17.4 1.0 CG A:ASP249 3.2 14.5 1.0 OD1 A:ASP198 3.4 12.8 1.0 O A:HOH427 3.5 23.5 1.0 CB A:ASP249 3.7 2.9 1.0 OE1 A:GLU224 3.8 10.2 1.0 CG A:GLU224 3.8 7.8 1.0 NZ A:LYS167 3.8 17.8 1.0 OD1 A:ASN200 4.0 25.7 1.0 OE2 A:GLU250 4.0 25.4 1.0 O A:HOH518 4.1 51.5 1.0 NZ A:LYS273 4.1 7.6 1.0 OE1 A:GLU250 4.2 7.2 1.0 O A:HOH485 4.2 34.2 1.0 OD1 A:ASP249 4.3 15.2 1.0 CD A:GLU250 4.5 13.1 1.0 CB A:ASP198 4.6 4.3 1.0 O A:HOH514 4.7 48.4 1.0 CE A:LYS167 4.8 15.6 1.0 CE A:LYS273 4.8 17.1 1.0 O A:HOH520 4.9 46.7 1.0 CG A:ASN200 4.9 21.8 1.0 CB A:GLU224 5.0 4.3 1.0

Manganese binding site 2 out of 2 in the Structure of Muconate Lactonizing Enzyme at 1.85 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Structure of Muconate Lactonizing Enzyme at 1.85 Angstroms Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn374 b:18.8 occ:1.00 O B:HOH451 1.7 26.4 1.0 O B:HOH390 2.1 10.6 1.0 OE2 B:GLU224 2.1 14.3 1.0 O B:HOH412 2.1 23.6 1.0 OD2 B:ASP249 2.2 12.1 1.0 OD2 B:ASP198 2.3 15.5 1.0 CD B:GLU224 3.0 16.6 1.0 CG B:ASP198 3.1 11.3 1.0 CG B:ASP249 3.3 22.6 1.0 OD1 B:ASP198 3.3 19.1 1.0 O B:HOH439 3.5 35.5 1.0 CB B:ASP249 3.7 8.7 1.0 OE1 B:GLU224 3.8 12.3 1.0 CG B:GLU224 3.8 13.1 1.0 NZ B:LYS167 4.0 17.4 1.0 OD1 B:ASN200 4.0 37.5 1.0 OE2 B:GLU250 4.1 36.8 1.0 OE1 B:GLU250 4.1 15.8 1.0 NZ B:LYS273 4.1 12.1 1.0 OD1 B:ASP249 4.4 11.8 1.0 CD B:GLU250 4.5 27.5 1.0 CB B:ASP198 4.5 11.1 1.0 CG B:ASN200 4.8 42.9 1.0 CE B:LYS273 4.9 10.5 1.0 CE B:LYS167 4.9 16.1 1.0 O B:HOH452 5.0 33.5 1.0 CB B:GLU224 5.0 6.9 1.0

S.Helin, P.C.Kahn, B.L.Guha, D.G.Mallows, A.Goldman. The Refined X-Ray Structure of Muconate Lactonizing Enzyme From Pseudomonas Putida PRS2000 at 1.85 A Resolution. J.Mol.Biol. V. 254 918 1995.
ISSN: ISSN 0022-2836
PubMed: 7500361
DOI: 10.1006/JMBI.1995.0666