Manganese in PDB 4fcx: S.Pombe MRE11 Apoenzym

The structure of S.Pombe MRE11 Apoenzym, PDB code: 4fcx was solved by C.B.Schiller, K.Lammens, K.P.Hopfner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	21.84 / 3.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	76.408, 82.262, 164.296, 90.00, 90.00, 90.00
R / Rfree (%)	22.7 / 28.6

The binding sites of Manganese atom in the S.Pombe MRE11 Apoenzym (pdb code 4fcx). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the S.Pombe MRE11 Apoenzym, PDB code: 4fcx:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in the S.Pombe MRE11 Apoenzym


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of S.Pombe MRE11 Apoenzym within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn501 b:49.9 occ:1.00 OD2 B:ASP25 2.2 59.1 1.0 NE2 B:HIS252 2.4 58.9 1.0 OD1 B:ASP65 2.5 58.2 1.0 NE2 B:HIS27 2.5 58.9 1.0 MN B:MN502 3.2 50.0 1.0 CD2 B:HIS252 3.2 57.9 1.0 CG B:ASP65 3.4 63.4 1.0 CG B:ASP25 3.4 61.7 1.0 CE1 B:HIS252 3.4 62.9 1.0 CE1 B:HIS27 3.4 59.3 1.0 CD2 B:HIS27 3.5 59.0 1.0 O B:HIS250 3.6 56.5 1.0 CB B:ASP65 3.8 62.1 1.0 CB B:ASP25 4.0 58.9 1.0 CG B:HIS252 4.4 57.1 1.0 OD1 B:ASP25 4.4 64.1 1.0 OD2 B:ASP65 4.5 67.3 1.0 ND1 B:HIS252 4.5 59.6 1.0 NE2 B:HIS222 4.5 59.5 1.0 C B:HIS250 4.5 57.6 1.0 ND1 B:HIS27 4.6 59.9 1.0 CE1 B:HIS222 4.6 61.3 1.0 CG B:HIS27 4.6 62.3 1.0 CA B:HIS250 4.7 58.1 1.0 OD1 B:ASN133 4.7 73.3 1.0 CA B:ASP25 5.0 56.8 1.0

Manganese binding site 2 out of 4 in the S.Pombe MRE11 Apoenzym


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of S.Pombe MRE11 Apoenzym within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn502 b:50.0 occ:1.00 OD1 B:ASP65 2.3 58.2 1.0 NE2 B:HIS222 2.5 59.5 1.0 ND2 B:ASN133 2.5 70.8 1.0 ND1 B:HIS250 2.5 57.6 1.0 OD1 B:ASN133 2.8 73.3 1.0 CG B:ASN133 3.0 71.9 1.0 MN B:MN501 3.2 49.9 1.0 CE1 B:HIS250 3.2 60.2 1.0 CD2 B:HIS222 3.3 61.0 1.0 CG B:ASP65 3.3 63.4 1.0 CE1 B:HIS222 3.4 61.3 1.0 CG B:HIS250 3.6 56.2 1.0 CA B:HIS250 3.7 58.1 1.0 OD2 B:ASP65 3.9 67.3 1.0 CB B:HIS250 4.0 57.2 1.0 OD2 B:ASP25 4.0 59.1 1.0 O B:HIS250 4.0 56.5 1.0 C B:HIS250 4.3 57.6 1.0 NE2 B:HIS250 4.4 62.7 1.0 CG B:HIS222 4.4 62.4 1.0 ND1 B:HIS222 4.4 62.1 1.0 N B:ASN133 4.5 63.4 1.0 CB B:ASP65 4.5 62.1 1.0 CB B:ASN133 4.5 70.8 1.0 CD2 B:HIS250 4.6 59.0 1.0 N B:HIS250 4.6 56.4 1.0

Manganese binding site 3 out of 4 in the S.Pombe MRE11 Apoenzym


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of S.Pombe MRE11 Apoenzym within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn501 b:58.0 occ:1.00 OD2 A:ASP65 2.2 59.5 1.0 CE1 A:HIS222 2.5 56.9 1.0 ND1 A:HIS250 2.5 52.7 1.0 ND2 A:ASN133 2.9 59.8 1.0 NE2 A:HIS222 3.1 55.6 1.0 MN A:MN502 3.1 64.0 1.0 CG A:ASP65 3.2 60.8 1.0 CE1 A:HIS250 3.3 55.3 1.0 OD1 A:ASP65 3.6 61.6 1.0 CG A:HIS250 3.6 53.4 1.0 ND1 A:HIS222 3.6 58.6 1.0 CG A:ASN133 4.0 73.1 1.0 CB A:HIS250 4.0 55.8 1.0 OD2 A:ASP25 4.0 61.0 1.0 CA A:HIS250 4.0 56.9 1.0 OD1 A:ASN133 4.3 75.9 1.0 CD2 A:HIS222 4.4 57.3 1.0 NE2 A:HIS250 4.5 54.1 1.0 CB A:ASP65 4.5 59.8 1.0 O A:HIS250 4.5 54.4 1.0 CD2 A:HIS250 4.6 51.7 1.0 CG A:HIS222 4.6 57.8 1.0 N A:ASN133 4.8 62.6 1.0 C A:HIS250 4.8 51.5 1.0

Manganese binding site 4 out of 4 in the S.Pombe MRE11 Apoenzym


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of S.Pombe MRE11 Apoenzym within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn502 b:64.0 occ:1.00 OD2 A:ASP65 2.3 59.5 1.0 OD2 A:ASP25 2.3 61.0 1.0 NE2 A:HIS252 2.4 54.8 1.0 NE2 A:HIS27 2.5 55.1 1.0 MN A:MN501 3.1 58.0 1.0 CD2 A:HIS252 3.2 57.1 1.0 CG A:ASP65 3.3 60.8 1.0 CE1 A:HIS27 3.5 54.4 1.0 CD2 A:HIS27 3.5 58.2 1.0 CG A:ASP25 3.5 61.2 1.0 CE1 A:HIS252 3.5 57.8 1.0 CB A:ASP65 3.7 59.8 1.0 CB A:ASP25 4.1 59.4 1.0 OD1 A:ASP65 4.4 61.6 1.0 CG A:HIS252 4.4 55.1 1.0 OD1 A:ASP25 4.5 65.9 1.0 ND1 A:HIS252 4.6 58.7 1.0 NE2 A:HIS222 4.6 55.6 1.0 ND1 A:HIS27 4.6 54.9 1.0 CG A:HIS27 4.6 59.2 1.0 CA A:HIS250 4.8 56.9 1.0 CE1 A:HIS222 4.8 56.9 1.0 ND1 A:HIS250 4.9 52.7 1.0 O A:HIS250 4.9 54.4 1.0

C.B.Schiller, K.Lammens, I.Guerini, B.Coordes, H.Feldmann, F.Schlauderer, C.Mockel, A.Schele, K.Strasser, S.P.Jackson, K.P.Hopfner. Structure of MRE11-NBS1 Complex Yields Insights Into Ataxia-Telangiectasia-Like Disease Mutations and Dna Damage Signaling. Nat.Struct.Mol.Biol. V. 19 693 2012.
ISSN: ISSN 1545-9993
PubMed: 22705791
DOI: 10.1038/NSMB.2323