Manganese in PDB 1fi2: Crystal Structure of Germin (Oxalate Oxidase)

All present enzymatic activity of Crystal Structure of Germin (Oxalate Oxidase):
1.2.3.4;

The structure of Crystal Structure of Germin (Oxalate Oxidase), PDB code: 1fi2 was solved by E.J.Woo, J.M.Dunwell, P.W.Goodenough, A.C.Marvier, R.W.Pickersgill, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	12.40 / 1.60
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	95.593, 95.593, 107.109, 90.00, 90.00, 120.00
R / Rfree (%)	19.6 / 23.3

The binding sites of Manganese atom in the Crystal Structure of Germin (Oxalate Oxidase) (pdb code 1fi2). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Crystal Structure of Germin (Oxalate Oxidase), PDB code: 1fi2:

Manganese binding site 1 out of 1 in the Crystal Structure of Germin (Oxalate Oxidase)


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 Germin (Oxalate Oxidase) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn202 b:4.5 occ:1.00 OE1 A:GLU95 2.2 3.6 1.0 O A:HOH223 2.2 2.4 1.0 NE2 A:HIS137 2.2 3.5 1.0 NE2 A:HIS88 2.3 4.7 1.0 NE2 A:HIS90 2.3 3.4 1.0 O A:HOH213 2.4 5.7 1.0 CD2 A:HIS137 3.1 3.2 1.0 CD A:GLU95 3.1 3.3 1.0 CD2 A:HIS90 3.2 3.1 1.0 CD2 A:HIS88 3.2 4.7 1.0 CE1 A:HIS88 3.2 4.9 1.0 CE1 A:HIS137 3.3 3.1 1.0 CE1 A:HIS90 3.4 3.7 1.0 OE2 A:GLU95 3.4 3.2 1.0 O A:HOH310 4.2 13.3 1.0 CG A:HIS137 4.3 3.2 1.0 ND1 A:HIS137 4.3 3.3 1.0 ND1 A:HIS88 4.3 4.4 1.0 CG A:HIS88 4.4 4.7 1.0 CG A:HIS90 4.4 3.4 1.0 ND1 A:HIS90 4.4 3.4 1.0 CG A:GLU95 4.5 3.5 1.0 CE2 A:PHE153 4.7 3.2 1.0 O A:HOH367 4.7 21.0 1.0 CB A:GLU95 4.8 4.2 1.0 ND2 A:ASN85 4.8 6.1 1.0 NE2 A:GLN139 4.9 6.8 1.0 CZ A:PHE153 4.9 3.3 1.0

E.J.Woo, J.M.Dunwell, P.W.Goodenough, A.C.Marvier, R.W.Pickersgill. Germin Is A Manganese Containing Homohexamer with Oxalate Oxidase and Superoxide Dismutase Activities. Nat.Struct.Biol. V. 7 1036 2000.
ISSN: ISSN 1072-8368
PubMed: 11062559
DOI: 10.1038/80954