Manganese in PDB 3fcm: Crystal Structure of A Nudix Hydrolase From Clostridium Perfringens

The structure of Crystal Structure of A Nudix Hydrolase From Clostridium Perfringens, PDB code: 3fcm was solved by K.Palani, S.K.Burley, S.Swaninathan, New York Sgx Research Center Forstructural Genomics (Nysgxrc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.48 / 2.20
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	80.395, 132.459, 41.361, 90.00, 90.00, 90.00
R / Rfree (%)	22.9 / 28

The binding sites of Manganese atom in the Crystal Structure of A Nudix Hydrolase From Clostridium Perfringens (pdb code 3fcm). 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 A Nudix Hydrolase From Clostridium Perfringens, PDB code: 3fcm:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of A Nudix Hydrolase From Clostridium Perfringens


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 A Nudix Hydrolase From Clostridium Perfringens within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn201 b:17.9 occ:1.00 NE2 A:HIS75 2.2 19.6 1.0 CE1 A:HIS43 2.3 15.4 1.0 NE2 A:HIS129 2.4 19.2 1.0 NE2 A:HIS127 2.5 15.2 1.0 O A:HOH208 2.5 17.6 1.0 NE2 A:HIS43 2.8 17.1 1.0 CD2 A:HIS75 3.0 17.3 1.0 CD2 A:HIS129 3.2 16.4 1.0 CE1 A:HIS75 3.3 21.1 1.0 CD2 A:HIS127 3.3 13.3 1.0 CE1 A:HIS129 3.4 16.5 1.0 CE1 A:HIS127 3.5 14.3 1.0 ND1 A:HIS43 3.6 19.6 1.0 CD2 A:HIS43 4.1 16.5 1.0 CG A:HIS75 4.2 21.0 1.0 ND1 A:HIS75 4.3 21.9 1.0 CG A:HIS129 4.4 15.5 1.0 O A:HOH224 4.5 19.2 1.0 ND1 A:HIS129 4.5 18.2 1.0 CG A:HIS43 4.5 18.0 1.0 CG A:HIS127 4.5 11.5 1.0 ND1 A:HIS127 4.6 13.9 1.0 CG2 A:VAL114 4.9 13.6 1.0 O A:HOH245 4.9 21.6 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of A Nudix Hydrolase From Clostridium Perfringens


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 A Nudix Hydrolase From Clostridium Perfringens within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn202 b:16.8 occ:1.00 NE2 B:HIS129 2.1 8.2 1.0 NE2 B:HIS127 2.2 11.9 1.0 CE1 B:HIS43 2.3 9.3 1.0 NE2 B:HIS75 2.3 17.5 1.0 O B:HOH204 2.4 13.5 1.0 NE2 B:HIS43 3.0 8.1 1.0 CD2 B:HIS129 3.0 9.7 1.0 CE1 B:HIS129 3.1 9.8 1.0 CE1 B:HIS127 3.2 10.0 1.0 CD2 B:HIS127 3.2 8.0 1.0 CD2 B:HIS75 3.2 19.1 1.0 CE1 B:HIS75 3.3 21.2 1.0 ND1 B:HIS43 3.4 15.0 1.0 ND1 B:HIS129 4.2 11.6 1.0 CG B:HIS129 4.2 9.7 1.0 ND1 B:HIS127 4.3 11.8 1.0 CD2 B:HIS43 4.3 9.2 1.0 CG B:HIS127 4.3 10.8 1.0 ND1 B:HIS75 4.4 22.1 1.0 CG B:HIS75 4.4 20.6 1.0 CG B:HIS43 4.5 13.4 1.0 CG2 B:VAL114 4.7 9.8 1.0 O B:HOH260 4.9 15.4 1.0 CG B:ARG37 4.9 20.5 1.0

K.Palani, S.K.Burley, S.Swaminathan. Crystal Structure of A Nudix Hydrolase From Clostridium Perfringens To Be Published.