Manganese in PDB 2muc: Muconate Cycloisomerase Variant F329I

All present enzymatic activity of Muconate Cycloisomerase Variant F329I:
5.5.1.1;

The structure of Muconate Cycloisomerase Variant F329I, PDB code: 2muc was solved by U.Schell, S.Helin, T.Kajander, M.Schlomann, A.Goldman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.30
Space group	I 4
Cell size a, b, c (Å), α, β, γ (°)	139.100, 139.100, 84.000, 90.00, 90.00, 90.00
R / Rfree (%)	17.4 / 21.6

The binding sites of Manganese atom in the Muconate Cycloisomerase Variant F329I (pdb code 2muc). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Muconate Cycloisomerase Variant F329I, PDB code: 2muc:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Muconate Cycloisomerase Variant F329I


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Muconate Cycloisomerase Variant F329I within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn380 b:17.6 occ:1.00 O A:HOH3143 2.3 23.9 1.0 OD2 A:ASP249 2.4 9.1 1.0 O A:HOH3144 2.4 22.9 1.0 O A:HOH3095 2.4 14.2 1.0 OE2 A:GLU224 2.5 10.1 1.0 OD2 A:ASP198 2.6 25.9 1.0 CD A:GLU224 3.1 6.8 1.0 CG A:ASP249 3.3 9.0 1.0 CG A:ASP198 3.3 16.8 1.0 O A:HOH3002 3.4 25.2 1.0 OD1 A:ASP198 3.5 19.7 1.0 CB A:ASP249 3.7 8.9 1.0 CG A:GLU224 3.7 2.0 1.0 OE1 A:GLU224 3.8 6.8 1.0 NZ A:LYS167 3.9 8.5 1.0 NZ A:LYS273 4.1 6.5 1.0 OE2 A:GLU250 4.2 24.6 1.0 OD1 A:ASN200 4.2 18.1 1.0 OE1 A:GLU250 4.3 12.7 1.0 OD1 A:ASP249 4.5 16.8 1.0 O A:HOH3135 4.5 42.6 1.0 CD A:GLU250 4.7 19.5 1.0 CB A:ASP198 4.7 6.8 1.0 CE A:LYS273 4.8 15.7 1.0 CE A:LYS167 4.9 12.0 1.0 CG A:ASN200 5.0 19.4 1.0

Manganese binding site 2 out of 2 in the Muconate Cycloisomerase Variant F329I


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Muconate Cycloisomerase Variant F329I within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn381 b:21.4 occ:1.00 O B:HOH4137 2.3 42.9 1.0 OD2 B:ASP249 2.4 10.3 1.0 O B:HOH4125 2.4 15.0 1.0 OE2 B:GLU224 2.4 10.5 1.0 O B:HOH4085 2.5 18.1 1.0 OD2 B:ASP198 2.5 24.1 1.0 CD B:GLU224 3.1 7.9 1.0 CG B:ASP198 3.2 15.0 1.0 OD1 B:ASP198 3.3 24.9 1.0 CG B:ASP249 3.4 8.6 1.0 O B:HOH4074 3.4 29.9 1.0 CG B:GLU224 3.7 2.6 1.0 CB B:ASP249 3.7 5.9 1.0 OE1 B:GLU224 3.8 7.6 1.0 NZ B:LYS167 3.9 15.1 1.0 O B:HOH4090 4.0 43.3 1.0 OD1 B:ASN200 4.2 22.4 1.0 NZ B:LYS273 4.2 11.7 1.0 OE2 B:GLU250 4.3 22.9 1.0 OE1 B:GLU250 4.3 14.0 1.0 OD1 B:ASP249 4.5 17.2 1.0 CB B:ASP198 4.6 13.6 1.0 CD B:GLU250 4.7 16.9 1.0 CE B:LYS167 4.8 17.2 1.0 CE B:LYS273 4.9 12.7 1.0 CB B:GLU224 5.0 3.3 1.0 CG B:ASN200 5.0 19.2 1.0

U.Schell, S.Helin, T.Kajander, M.Schlomann, A.Goldman. Structural Basis For the Activity of Two Muconate Cycloisomerase Variants Toward Substituted Muconates. Proteins V. 34 125 1999.
ISSN: ISSN 0887-3585
PubMed: 10336378
DOI: 10.1002/(SICI)1097-0134(19990101)34:1<125::AID-PROT10>3.3.CO;2-P