Manganese in PDB 4hr0: R2-Like Ligand-Binding Oxidase with Aerobically Reconstituted Metal Cofactor

All present enzymatic activity of R2-Like Ligand-Binding Oxidase with Aerobically Reconstituted Metal Cofactor:
1.17.4.1;

The structure of R2-Like Ligand-Binding Oxidase with Aerobically Reconstituted Metal Cofactor, PDB code: 4hr0 was solved by J.J.Griese, M.Hogbom, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.15 / 1.90
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	56.150, 97.738, 130.850, 90.00, 90.00, 90.00
R / Rfree (%)	16.6 / 19.6

The structure of R2-Like Ligand-Binding Oxidase with Aerobically Reconstituted Metal Cofactor also contains other interesting chemical elements:

Iron	(Fe)	1 atom
Sodium	(Na)	1 atom

The binding sites of Manganese atom in the R2-Like Ligand-Binding Oxidase with Aerobically Reconstituted Metal Cofactor (pdb code 4hr0). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the R2-Like Ligand-Binding Oxidase with Aerobically Reconstituted Metal Cofactor, PDB code: 4hr0:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the R2-Like Ligand-Binding Oxidase with Aerobically Reconstituted Metal Cofactor


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of R2-Like Ligand-Binding Oxidase with Aerobically Reconstituted Metal Cofactor within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn401 b:27.8 occ:1.00 O2 A:PLM405 1.9 41.4 1.0 OE2 A:GLU102 2.1 25.8 1.0 O A:HOH502 2.1 32.4 1.0 OE2 A:GLU69 2.2 31.2 1.0 ND1 A:HIS105 2.2 23.8 1.0 O A:HOH562 2.4 35.8 1.0 C1 A:PLM405 2.7 39.7 1.0 CE1 A:HIS105 3.0 26.2 1.0 O1 A:PLM405 3.1 41.9 1.0 HE1 A:HIS105 3.1 26.2 1.0 CD A:GLU69 3.1 36.5 1.0 CD A:GLU102 3.1 28.9 1.0 CG A:HIS105 3.3 24.4 1.0 OE1 A:GLU69 3.4 39.8 1.0 OE1 A:GLU102 3.4 29.6 1.0 HB2 A:HIS105 3.5 26.3 1.0 FE A:FE402 3.5 30.8 1.0 HB3 A:HIS105 3.6 26.3 1.0 CB A:HIS105 3.7 26.3 1.0 HA A:GLU102 3.7 26.3 1.0 HG21 A:VAL72 4.0 27.0 1.0 OE1 A:GLU202 4.0 36.0 1.0 HG A:LEU198 4.1 29.7 1.0 C2 A:PLM405 4.1 38.1 1.0 HE1 A:HIS205 4.2 26.2 1.0 HH A:TYR175 4.2 33.3 1.0 HA A:GLU69 4.2 26.6 1.0 NE2 A:HIS105 4.2 26.4 1.0 H31 A:PLM405 4.2 39.5 1.0 H32 A:PLM405 4.3 39.5 1.0 CD2 A:HIS105 4.4 25.5 1.0 C3 A:PLM405 4.5 39.5 1.0 CG A:GLU102 4.5 26.0 1.0 CG A:GLU69 4.5 28.1 1.0 OH A:TYR175 4.5 33.3 1.0 HB3 A:GLU69 4.6 26.5 1.0 CA A:GLU102 4.6 26.3 1.0 H22 A:PLM405 4.7 38.1 1.0 HB3 A:GLU102 4.7 25.9 1.0 CG2 A:VAL72 4.8 27.0 1.0 CD A:GLU202 4.8 39.3 1.0 OE2 A:GLU202 4.8 32.5 1.0 CE1 A:HIS205 4.8 26.2 1.0 H21 A:PLM405 4.8 38.1 1.0 HG22 A:VAL72 4.9 27.0 1.0 HD23 A:LEU198 4.9 32.8 1.0 CB A:GLU102 4.9 25.9 1.0 HG23 A:VAL72 4.9 27.0 1.0 ND1 A:HIS205 4.9 25.6 1.0 HG3 A:GLU69 4.9 28.1 1.0 CB A:GLU69 4.9 26.5 1.0 HE2 A:HIS105 5.0 26.4 1.0 CG A:LEU198 5.0 29.7 1.0

Manganese binding site 2 out of 2 in the R2-Like Ligand-Binding Oxidase with Aerobically Reconstituted Metal Cofactor


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of R2-Like Ligand-Binding Oxidase with Aerobically Reconstituted Metal Cofactor within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn403 b:76.8 occ:0.62 NE2 A:HIS130 2.3 43.5 1.0 CE1 A:HIS130 3.2 41.0 1.0 CD2 A:HIS130 3.2 42.3 1.0 HE1 A:HIS130 3.4 41.0 1.0 HD2 A:HIS130 3.4 42.3 1.0 O A:HOH542 4.1 41.2 1.0 ND1 A:HIS130 4.3 39.8 1.0 CG A:HIS130 4.4 40.5 1.0 HA3 A:GLY240 4.7 35.0 1.0 O A:HOH581 4.7 42.1 1.0 OD1 A:ASP129 4.8 49.2 1.0 HA2 A:GLY240 5.0 35.0 1.0

J.J.Griese, K.Roos, N.Cox, H.S.Shafaat, R.M.M.Branca, J.Lehtio, A.Graslund, W.Lubitz, P.E.M.Siegbahn, M.Hogbom. Direct Observation of Structurally Encoded Metal Discrimination and Ether Bond Formation in A Heterodinuclear Metalloprotein Proc.Natl.Acad.Sci.Usa V. 110 17189 2013.
ISSN: ISSN 0027-8424
PubMed: 24101498
DOI: 10.1073/PNAS.1304368110