Manganese in PDB 1f9c: Crystal Structure of Mle D178N Variant

All present enzymatic activity of Crystal Structure of Mle D178N Variant:
5.5.1.1;

The structure of Crystal Structure of Mle D178N Variant, PDB code: 1f9c was solved by T.Kajander, L.Lehtio, P.C.Kahn, A.Goldman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.50
Space group	I 4
Cell size a, b, c (Å), α, β, γ (°)	136.979, 136.979, 82.968, 90.00, 90.00, 90.00
R / Rfree (%)	18.7 / 23.4

The binding sites of Manganese atom in the Crystal Structure of Mle D178N Variant (pdb code 1f9c). 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 Mle D178N Variant, PDB code: 1f9c:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of Mle D178N Variant


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 Mle D178N Variant within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn374 b:12.2 occ:1.00 OD2 A:ASP249 2.2 10.3 1.0 OD2 A:ASP198 2.4 11.9 1.0 O A:HOH446 2.5 14.3 1.0 O A:HOH421 2.5 14.3 1.0 O A:HOH447 2.5 19.7 1.0 OE2 A:GLU224 2.5 22.8 1.0 CG A:ASP198 3.2 11.9 1.0 CG A:ASP249 3.2 10.3 1.0 CD A:GLU224 3.3 22.8 1.0 OD1 A:ASP198 3.3 11.9 1.0 CB A:ASP249 3.5 10.3 1.0 CG A:GLU224 3.8 22.8 1.0 NZ A:LYS273 3.9 15.3 1.0 OE2 A:GLU250 4.0 16.6 1.0 OE1 A:GLU250 4.1 16.6 1.0 OE1 A:GLU224 4.2 22.8 1.0 NZ A:LYS167 4.3 17.3 1.0 OD1 A:ASP249 4.4 10.3 1.0 CD A:GLU250 4.5 16.6 1.0 CE A:LYS273 4.5 15.3 1.0 ND2 A:ASN200 4.6 37.0 1.0 CB A:ASP198 4.6 11.9 1.0 OE2 A:GLU327 4.8 16.0 1.0 O A:HOH401 4.8 4.0 1.0 CB A:GLU224 4.9 22.8 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of Mle D178N Variant


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 Mle D178N Variant within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn374 b:12.8 occ:1.00 OD2 B:ASP249 2.3 4.1 1.0 OD2 B:ASP198 2.4 10.4 1.0 O B:HOH461 2.4 13.7 1.0 O B:HOH432 2.4 22.0 1.0 OE2 B:GLU224 2.5 10.4 1.0 O B:HOH440 2.5 9.3 1.0 CG B:ASP198 3.2 10.4 1.0 CD B:GLU224 3.2 10.4 1.0 CG B:ASP249 3.3 4.1 1.0 OD1 B:ASP198 3.3 10.4 1.0 CB B:ASP249 3.6 4.1 1.0 O B:HOH474 3.7 11.1 1.0 CG B:GLU224 3.8 10.4 1.0 NZ B:LYS273 3.9 9.5 1.0 OE1 B:GLU224 4.1 10.4 1.0 OE2 B:GLU250 4.1 12.9 1.0 OE1 B:GLU250 4.2 12.9 1.0 NZ B:LYS167 4.2 11.9 1.0 OD1 B:ASP249 4.4 4.1 1.0 CE B:LYS273 4.5 9.5 1.0 ND2 B:ASN200 4.6 35.5 1.0 CD B:GLU250 4.6 12.9 1.0 CB B:ASP198 4.6 10.4 1.0 OE2 B:GLU327 4.7 11.6 1.0 CB B:GLU224 4.9 10.4 1.0

T.Kajander, P.C.Kahn, S.H.Passila, D.C.Cohen, L.Lehtio, W.Adolfsen, J.Warwicker, U.Schell, A.Goldman. Buried Charged Surface in Proteins. Structure Fold.Des. V. 8 1203 2000.
ISSN: ISSN 0969-2126
PubMed: 11080642
DOI: 10.1016/S0969-2126(00)00520-7