Manganese in PDB 6qsb: Crystal Structure of ARG470HIS Mutant of Human Prolidase with Mn Ions

All present enzymatic activity of Crystal Structure of ARG470HIS Mutant of Human Prolidase with Mn Ions:
3.4.13.9;

The structure of Crystal Structure of ARG470HIS Mutant of Human Prolidase with Mn Ions, PDB code: 6qsb was solved by P.Wilk, E.Wator, M.S.Weiss, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	23.37 / 1.99
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	103.555, 108.533, 211.804, 90.00, 90.00, 90.00
R / Rfree (%)	18.8 / 22.3

The binding sites of Manganese atom in the Crystal Structure of ARG470HIS Mutant of Human Prolidase with Mn Ions (pdb code 6qsb). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Crystal Structure of ARG470HIS Mutant of Human Prolidase with Mn Ions, PDB code: 6qsb:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in the Crystal Structure of ARG470HIS Mutant of Human Prolidase with Mn Ions


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 ARG470HIS Mutant of Human Prolidase with Mn Ions within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn499 b:45.0 occ:0.97 NE2 A:HIS370 2.2 31.6 1.0 OE2 A:GLU412 2.3 35.0 1.0 OD2 A:ASP287 2.3 28.9 1.0 OE2 A:GLU452 2.4 32.0 1.0 HG21 A:THR410 3.0 38.7 1.0 HG1 A:THR410 3.1 32.5 1.0 CD A:GLU412 3.1 34.6 1.0 CD2 A:HIS370 3.2 24.2 1.0 CG A:ASP287 3.2 34.9 1.0 CE1 A:HIS370 3.2 29.6 1.0 HD2 A:HIS370 3.3 29.1 1.0 CD A:GLU452 3.4 32.2 1.0 O A:HOH819 3.4 48.7 1.0 HE1 A:HIS370 3.4 35.5 1.0 MN A:MN500 3.4 39.5 1.0 OE1 A:GLU412 3.4 37.3 1.0 OD1 A:ASP287 3.6 35.3 1.0 OE1 A:GLU452 3.6 34.8 1.0 O A:HOH915 3.8 44.0 1.0 CG2 A:THR410 3.8 32.2 1.0 HB A:THR410 3.9 36.7 1.0 OG1 A:THR410 3.9 27.0 1.0 CB A:THR410 4.1 30.6 1.0 ND1 A:HIS370 4.3 23.5 1.0 HG23 A:THR410 4.3 38.7 1.0 HB3 A:ASP287 4.3 42.5 1.0 CG A:HIS370 4.3 31.6 1.0 HD2 A:HIS377 4.3 41.9 1.0 CB A:ASP287 4.4 35.5 1.0 HG22 A:VAL376 4.4 41.0 1.0 CG A:GLU412 4.4 33.0 1.0 NE2 A:HIS377 4.4 35.8 1.0 HG22 A:THR410 4.5 38.7 1.0 HG2 A:GLU412 4.5 39.6 1.0 HB3 A:GLU412 4.7 43.3 1.0 CG A:GLU452 4.7 39.9 1.0 HG3 A:GLU452 4.7 47.9 1.0 CD2 A:HIS377 4.7 35.0 1.0 HB2 A:ASP287 4.8 42.5 1.0

Manganese binding site 2 out of 4 in the Crystal Structure of ARG470HIS Mutant of Human Prolidase with Mn Ions


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 ARG470HIS Mutant of Human Prolidase with Mn Ions within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn500 b:39.5 occ:0.96 OD1 A:ASP287 2.2 35.3 1.0 OD2 A:ASP276 2.2 33.0 1.0 OE1 A:GLU452 2.2 34.8 1.0 OD1 A:ASP276 2.4 31.4 1.0 CG A:ASP276 2.6 30.6 1.0 O A:HOH915 2.7 44.0 1.0 CG A:ASP287 3.1 34.9 1.0 CD A:GLU452 3.1 32.2 1.0 HG1 A:THR289 3.2 39.4 1.0 OE2 A:GLU452 3.4 32.0 1.0 OD2 A:ASP287 3.4 28.9 1.0 MN A:MN499 3.4 45.0 1.0 HH A:TYR241 3.6 41.6 1.0 OG1 A:THR289 3.6 32.8 1.0 OH A:TYR241 3.6 34.7 1.0 HE A:ARG450 3.9 45.4 1.0 HH21 A:ARG450 3.9 41.7 1.0 CB A:ASP276 4.1 31.1 1.0 CZ A:TYR241 4.1 36.4 1.0 O A:HOH819 4.3 48.7 1.0 OE1 A:GLU412 4.4 37.3 1.0 HE2 A:TYR241 4.4 45.7 1.0 HB2 A:ASP276 4.4 37.4 1.0 CE2 A:TYR241 4.4 38.1 1.0 CB A:ASP287 4.5 35.5 1.0 H A:ILE288 4.5 34.1 1.0 HB3 A:ASP276 4.5 37.4 1.0 CG A:GLU452 4.5 39.9 1.0 HA A:ASP287 4.5 39.5 1.0 N A:ILE288 4.6 28.4 1.0 NE A:ARG450 4.7 37.9 1.0 O A:ILE288 4.7 27.4 1.0 NH2 A:ARG450 4.7 34.7 1.0 C A:ASP287 4.7 32.2 1.0 HD12 A:ILE244 4.7 47.4 1.0 HA A:ASP276 4.7 34.5 1.0 CE1 A:TYR241 4.8 29.8 1.0 HB2 A:GLU452 4.8 33.8 1.0 HB3 A:GLU452 4.8 33.8 1.0 HG2 A:GLU452 4.8 47.9 1.0 CA A:ASP287 4.8 32.9 1.0 C A:ILE288 4.8 34.7 1.0 OE2 A:GLU412 4.9 35.0 1.0 HB3 A:ASP287 4.9 42.5 1.0 HE1 A:TYR241 4.9 35.7 1.0 CD A:GLU412 4.9 34.6 1.0 CA A:ASP276 4.9 28.8 1.0 CB A:GLU452 5.0 28.1 1.0 CB A:THR289 5.0 30.6 1.0

Manganese binding site 3 out of 4 in the Crystal Structure of ARG470HIS Mutant of Human Prolidase with Mn Ions


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of ARG470HIS Mutant of Human Prolidase with Mn Ions within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn499 b:47.6 occ:0.95 NE2 B:HIS370 2.3 27.3 1.0 OE2 B:GLU452 2.3 29.1 1.0 OE2 B:GLU412 2.4 39.5 1.0 OD2 B:ASP287 2.4 29.3 1.0 HG21 B:THR410 2.9 42.0 1.0 CD B:GLU412 3.1 35.8 1.0 O B:HOH806 3.1 47.4 1.0 HG1 B:THR410 3.2 40.0 1.0 CG B:ASP287 3.2 34.5 1.0 CD2 B:HIS370 3.3 31.8 1.0 OE1 B:GLU412 3.3 33.2 1.0 CE1 B:HIS370 3.3 28.8 1.0 CD B:GLU452 3.4 32.9 1.0 HD2 B:HIS370 3.4 38.2 1.0 MN B:MN500 3.4 39.8 1.0 HE1 B:HIS370 3.5 34.5 1.0 OD1 B:ASP287 3.6 35.8 1.0 OE1 B:GLU452 3.8 40.7 1.0 CG2 B:THR410 3.8 35.0 1.0 O B:HOH910 3.9 40.1 1.0 HB B:THR410 3.9 35.6 1.0 OG1 B:THR410 4.0 33.3 1.0 CB B:THR410 4.1 29.7 1.0 HB3 B:ASP287 4.3 34.7 1.0 HG23 B:THR410 4.3 42.0 1.0 HG22 B:THR410 4.3 42.0 1.0 HD2 B:HIS377 4.4 33.2 1.0 CB B:ASP287 4.4 28.9 1.0 ND1 B:HIS370 4.4 31.7 1.0 CG B:HIS370 4.4 28.7 1.0 HG22 B:VAL376 4.4 40.0 1.0 CG B:GLU412 4.5 32.5 1.0 NE2 B:HIS377 4.5 38.5 1.0 HG2 B:GLU412 4.6 39.0 1.0 HG3 B:GLU452 4.6 42.4 1.0 CG B:GLU452 4.7 35.4 1.0 HB3 B:GLU412 4.7 37.0 1.0 CD2 B:HIS377 4.8 27.7 1.0 HB2 B:ASP287 4.8 34.7 1.0

Manganese binding site 4 out of 4 in the Crystal Structure of ARG470HIS Mutant of Human Prolidase with Mn Ions


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystal Structure of ARG470HIS Mutant of Human Prolidase with Mn Ions within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn500 b:39.8 occ:0.97 OD2 B:ASP276 2.1 37.5 1.0 OD1 B:ASP287 2.1 35.8 1.0 OE1 B:GLU452 2.2 40.7 1.0 OD1 B:ASP276 2.3 28.8 1.0 CG B:ASP276 2.4 34.1 1.0 O B:HOH910 2.7 40.1 1.0 CD B:GLU452 3.0 32.9 1.0 CG B:ASP287 3.0 34.5 1.0 OE2 B:GLU452 3.2 29.1 1.0 HG1 B:THR289 3.2 37.4 1.0 OD2 B:ASP287 3.3 29.3 1.0 MN B:MN499 3.4 47.6 0.9 HH B:TYR241 3.6 45.7 1.0 OG1 B:THR289 3.6 31.1 1.0 OH B:TYR241 3.7 38.1 1.0 CB B:ASP276 3.9 28.4 1.0 HH21 B:ARG450 4.0 38.4 1.0 HE B:ARG450 4.1 36.6 1.0 CZ B:TYR241 4.1 36.7 1.0 HB2 B:ASP276 4.3 34.0 1.0 HE2 B:TYR241 4.4 46.7 1.0 HB3 B:ASP276 4.4 34.0 1.0 CG B:GLU452 4.4 35.4 1.0 OE1 B:GLU412 4.4 33.2 1.0 CB B:ASP287 4.4 28.9 1.0 CE2 B:TYR241 4.4 38.9 1.0 H B:ILE288 4.4 34.6 1.0 HA B:ASP287 4.5 40.4 1.0 N B:ILE288 4.5 28.8 1.0 O B:HOH806 4.6 47.4 1.0 O B:ILE288 4.6 32.0 1.0 C B:ASP287 4.6 34.8 1.0 HG2 B:GLU452 4.6 42.4 1.0 HA B:ASP276 4.6 29.5 1.0 CE1 B:TYR241 4.7 33.7 1.0 NH2 B:ARG450 4.7 32.0 1.0 C B:ILE288 4.7 37.8 1.0 CA B:ASP287 4.8 33.7 1.0 HB3 B:GLU452 4.8 42.0 1.0 HB3 B:ASP287 4.8 34.7 1.0 HD12 B:ILE244 4.8 50.5 1.0 CA B:ASP276 4.8 24.6 1.0 NE B:ARG450 4.8 30.5 1.0 HB2 B:GLU452 4.8 42.0 1.0 HE1 B:TYR241 4.9 40.4 1.0 CB B:GLU452 5.0 35.0 1.0 CB B:THR289 5.0 26.9 1.0

P.Wilk, E.Wator, M.S.Weiss. Crystal Structure of ARG470HIS Mutant of Human Prolidase with Mn Ions To Be Published.