Manganese in PDB 8vag: Crystal Structure of Mnii/Mnii Ctcadd From Chlamydia Trachomatis

The structure of Crystal Structure of Mnii/Mnii Ctcadd From Chlamydia Trachomatis, PDB code: 8vag was solved by H.N.Phan, P.D.Swartz, T.M.Makris, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	17.14 / 2.61
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	91.668, 91.668, 117.602, 90, 90, 120
R / Rfree (%)	22.2 / 29.8

The binding sites of Manganese atom in the Crystal Structure of Mnii/Mnii Ctcadd From Chlamydia Trachomatis (pdb code 8vag). 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 Mnii/Mnii Ctcadd From Chlamydia Trachomatis, PDB code: 8vag:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in the Crystal Structure of Mnii/Mnii Ctcadd From Chlamydia Trachomatis


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 Mnii/Mnii Ctcadd From Chlamydia Trachomatis within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn301 b:38.9 occ:0.60 NE2 A:HIS174 2.1 50.4 1.0 O A:HOH407 2.2 35.1 0.6 OE2 A:GLU81 2.2 40.2 1.0 ND1 A:HIS88 2.4 43.9 1.0 OE1 A:GLU81 2.6 38.0 1.0 CD A:GLU81 2.6 41.5 1.0 CE1 A:HIS174 2.8 45.4 1.0 CD2 A:HIS174 3.2 50.6 1.0 CE1 A:HIS88 3.2 45.7 1.0 CG A:HIS88 3.4 39.1 1.0 CB A:HIS88 3.7 37.7 1.0 ND1 A:HIS174 4.0 48.9 1.0 MN A:MN302 4.0 53.2 1.0 CG A:GLU81 4.0 37.2 1.0 CG A:HIS174 4.2 48.7 1.0 O A:HOH404 4.2 41.7 1.0 NE2 A:HIS88 4.4 41.0 1.0 OH A:TYR170 4.4 44.4 1.0 CD2 A:HIS88 4.4 41.6 1.0 CB A:GLU81 4.9 35.5 1.0 CE2 A:TYR170 4.9 41.1 1.0 CZ A:TYR170 4.9 44.9 1.0 CA A:GLU81 5.0 33.9 1.0

Manganese binding site 2 out of 4 in the Crystal Structure of Mnii/Mnii Ctcadd From Chlamydia Trachomatis


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 Mnii/Mnii Ctcadd From Chlamydia Trachomatis within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn302 b:53.2 occ:1.00 OE2 A:GLU142 2.1 48.8 1.0 OD1 A:ASP178 2.2 40.6 1.0 O A:HOH407 2.2 35.1 0.6 ND1 A:HIS181 2.3 37.8 1.0 O A:HOH404 2.4 41.7 1.0 CE1 A:HIS181 3.0 43.9 1.0 CD A:GLU142 3.0 50.0 1.0 CG A:ASP178 3.2 41.6 1.0 CG A:HIS181 3.4 40.6 1.0 CG A:GLU142 3.5 38.9 1.0 OD2 A:ASP178 3.5 45.4 1.0 OE1 A:GLU81 3.6 38.0 1.0 CB A:HIS181 3.9 44.8 1.0 MN A:MN301 4.0 38.9 0.6 OD1 A:ASN77 4.0 37.4 1.0 OE1 A:GLU142 4.0 46.8 1.0 NE2 A:HIS181 4.2 35.2 1.0 CD2 A:HIS181 4.4 41.1 1.0 CB A:ASP178 4.5 43.4 1.0 CD A:GLU81 4.5 41.5 1.0 CD2 A:HIS174 4.6 50.6 1.0 CA A:ASP178 4.6 43.5 1.0 ND2 A:ASN77 4.6 48.3 1.0 NE2 A:HIS174 4.7 50.4 1.0 CG A:ASN77 4.7 39.2 1.0 OE2 A:GLU81 4.8 40.2 1.0 CE1 A:PHE54 4.9 39.7 1.0 CB A:GLU142 4.9 30.0 1.0

Manganese binding site 3 out of 4 in the Crystal Structure of Mnii/Mnii Ctcadd From Chlamydia Trachomatis


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 Mnii/Mnii Ctcadd From Chlamydia Trachomatis within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn301 b:51.8 occ:0.70 OE2 B:GLU81 2.1 48.1 1.0 O B:HOH421 2.1 34.8 0.7 ND1 B:HIS88 2.2 41.1 1.0 NE2 B:HIS174 2.2 44.3 1.0 OE1 B:GLU81 2.2 46.0 1.0 CD B:GLU81 2.4 44.8 1.0 O B:HOH401 2.5 39.2 0.7 CE1 B:HIS174 2.9 47.6 1.0 CE1 B:HIS88 3.0 44.3 1.0 CG B:HIS88 3.3 47.7 1.0 CD2 B:HIS174 3.4 42.2 1.0 CB B:HIS88 3.7 46.8 1.0 OH B:TYR170 3.8 45.5 1.0 CG B:GLU81 4.0 44.8 1.0 ND1 B:HIS174 4.1 47.3 1.0 NE2 B:HIS88 4.2 46.2 1.0 CD2 B:HIS88 4.3 45.4 1.0 CZ B:TYR170 4.3 45.5 1.0 CE2 B:TYR170 4.3 38.9 1.0 CG B:HIS174 4.4 43.1 1.0 MN B:MN302 4.7 50.2 1.0 O B:HOH404 4.7 44.1 1.0 CB B:GLU81 4.8 37.1 1.0 OE2 B:GLU142 4.9 49.8 1.0

Manganese binding site 4 out of 4 in the Crystal Structure of Mnii/Mnii Ctcadd From Chlamydia Trachomatis


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 Mnii/Mnii Ctcadd From Chlamydia Trachomatis within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn302 b:50.2 occ:1.00 OE2 B:GLU142 2.0 49.8 1.0 OD1 B:ASP178 2.1 47.6 1.0 ND1 B:HIS181 2.2 43.5 1.0 O B:HOH404 2.3 44.1 1.0 O B:HOH401 2.5 39.2 0.7 CD B:GLU142 2.6 46.1 1.0 OE1 B:GLU142 2.8 40.4 1.0 CE1 B:HIS181 3.1 40.2 1.0 CG B:ASP178 3.2 48.6 1.0 CG B:HIS181 3.3 43.2 1.0 OE2 B:GLU81 3.4 48.1 1.0 CB B:HIS181 3.7 41.6 1.0 OD2 B:ASP178 3.7 48.2 1.0 CG B:GLU142 3.9 38.6 1.0 OD1 B:ASN77 3.9 46.4 1.0 NE2 B:HIS181 4.3 41.0 1.0 CD2 B:HIS181 4.4 38.3 1.0 CB B:ASP178 4.4 46.3 1.0 CA B:ASP178 4.5 40.7 1.0 CD B:GLU81 4.6 44.8 1.0 CB B:GLU142 4.6 42.8 1.0 ND2 B:ASN77 4.6 42.8 1.0 CG B:ASN77 4.7 43.1 1.0 MN B:MN301 4.7 51.8 0.7 CE2 B:PHE54 4.8 40.7 1.0 O B:HOH421 4.8 34.8 0.7 O B:ALA177 5.0 38.9 1.0

H.N.Phan, P.D.Swartz, M.Gangopadhyay, Y.Guo, A.I.Smirnov, T.M.Makris. Assembly of A Heterobimetallic Fe/Mn Cofactor in the Para -Aminobenzoate Synthase Chlamydia Protein Associating with Death Domains (Cadd) Initiates Long-Range Radical Hole-Hopping. Biochemistry 2024.
ISSN: ISSN 0006-2960
PubMed: 39471288
DOI: 10.1021/ACS.BIOCHEM.4C00326