Manganese in PDB 3muc: Muconate Cycloisomerase Variant I54V

All present enzymatic activity of Muconate Cycloisomerase Variant I54V:
5.5.1.1;

The structure of Muconate Cycloisomerase Variant I54V, PDB code: 3muc 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 (°)	139.600, 139.600, 84.200, 90.00, 90.00, 90.00
R / Rfree (%)	17.6 / 22.3

The binding sites of Manganese atom in the Muconate Cycloisomerase Variant I54V (pdb code 3muc). 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 I54V, PDB code: 3muc:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Muconate Cycloisomerase Variant I54V


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 I54V within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn380 b:14.1 occ:1.00 O A:HOH3110 2.3 24.2 1.0 O A:HOH3060 2.3 10.9 1.0 O A:HOH3140 2.4 3.4 1.0 OD2 A:ASP249 2.4 8.4 1.0 OD2 A:ASP198 2.5 11.0 1.0 OE2 A:GLU224 2.6 12.0 1.0 CD A:GLU224 3.1 6.7 1.0 CG A:ASP198 3.3 8.8 1.0 OD1 A:ASP198 3.4 10.1 1.0 CG A:ASP249 3.4 8.1 1.0 O A:HOH3080 3.6 22.3 1.0 CB A:ASP249 3.7 4.8 1.0 CG A:GLU224 3.8 2.0 1.0 OE1 A:GLU224 3.8 7.5 1.0 NZ A:LYS167 4.0 6.2 1.0 OE2 A:GLU250 4.1 18.1 1.0 OD1 A:ASN200 4.2 17.8 1.0 NZ A:LYS273 4.2 10.2 1.0 OE1 A:GLU250 4.3 2.3 1.0 OD1 A:ASP249 4.5 13.2 1.0 CD A:GLU250 4.6 7.4 1.0 CB A:ASP198 4.7 4.8 1.0 O A:HOH3089 4.7 28.6 1.0 CG A:ASN200 4.9 14.8 1.0 CE A:LYS273 4.9 11.9 1.0 CE A:LYS167 5.0 12.9 1.0 CB A:GLU224 5.0 2.1 1.0

Manganese binding site 2 out of 2 in the Muconate Cycloisomerase Variant I54V


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 I54V within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn381 b:15.4 occ:1.00 O B:HOH4103 2.3 21.8 1.0 O B:HOH4079 2.4 5.7 1.0 O B:HOH4062 2.4 19.2 1.0 OD2 B:ASP249 2.4 8.1 1.0 OE2 B:GLU224 2.5 9.2 1.0 OD2 B:ASP198 2.5 11.1 1.0 CD B:GLU224 3.1 4.3 1.0 CG B:ASP198 3.3 9.2 1.0 OD1 B:ASP198 3.4 13.2 1.0 CG B:ASP249 3.4 5.3 1.0 O B:HOH4073 3.6 22.4 1.0 CG B:GLU224 3.7 2.0 1.0 CB B:ASP249 3.7 5.9 1.0 OE1 B:GLU224 3.8 5.4 1.0 NZ B:LYS167 4.0 16.2 1.0 OE2 B:GLU250 4.2 22.3 1.0 OD1 B:ASN200 4.3 15.8 1.0 OE1 B:GLU250 4.3 9.7 1.0 NZ B:LYS273 4.4 11.9 1.0 OD1 B:ASP249 4.6 12.1 1.0 CB B:ASP198 4.7 7.3 1.0 CD B:GLU250 4.7 12.3 1.0 CB B:GLU224 4.9 2.0 1.0 CE B:LYS273 4.9 10.5 1.0 O B:HOH4070 4.9 22.2 1.0 CE B:LYS167 5.0 11.2 1.0 CG B:ASN200 5.0 18.0 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