Manganese in PDB 6czo: The KNL1-PP1 Holoenzyme

All present enzymatic activity of The KNL1-PP1 Holoenzyme:
3.1.3.16;

The structure of The KNL1-PP1 Holoenzyme, PDB code: 6czo was solved by R.Bajaj, W.Peti, R.Page, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.13 / 2.95
Space group	P 42 21 2
Cell size a, b, c (Å), α, β, γ (°)	138.049, 138.049, 118.423, 90.00, 90.00, 90.00
R / Rfree (%)	16.9 / 21.3

The binding sites of Manganese atom in the The KNL1-PP1 Holoenzyme (pdb code 6czo). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the The KNL1-PP1 Holoenzyme, PDB code: 6czo:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in the The KNL1-PP1 Holoenzyme


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of The KNL1-PP1 Holoenzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn401 b:57.3 occ:1.00 OD2 A:ASP64 2.1 50.9 1.0 OD2 A:ASP92 2.2 61.3 1.0 O A:HOH501 2.2 73.8 1.0 NE2 A:HIS66 2.2 56.9 1.0 O A:HOH510 2.2 64.7 1.0 O1 A:PO4403 2.3 56.1 1.0 CE1 A:HIS66 3.1 49.4 1.0 MN A:MN402 3.1 47.7 1.0 CG A:ASP92 3.2 48.0 1.0 P A:PO4403 3.3 78.0 1.0 CD2 A:HIS66 3.3 52.2 1.0 CG A:ASP64 3.3 62.4 1.0 O4 A:PO4403 3.3 44.5 1.0 CB A:ASP92 3.7 46.7 1.0 O3 A:PO4403 3.7 68.6 1.0 CB A:ASP64 4.1 44.6 1.0 CD2 A:HIS125 4.2 42.7 1.0 ND1 A:HIS66 4.2 41.1 1.0 OH A:TYR272 4.2 66.8 1.0 OD1 A:ASP92 4.3 42.0 1.0 OD1 A:ASP64 4.3 61.9 1.0 NH1 A:ARG96 4.3 57.7 1.0 O A:HIS248 4.3 56.1 1.0 CG A:HIS66 4.4 42.9 1.0 CE1 A:HIS173 4.5 41.5 1.0 NE2 A:HIS173 4.5 39.3 1.0 NE2 A:HIS125 4.5 52.7 1.0 O2 A:PO4403 4.6 49.2 1.0 CE2 A:PHE267 4.6 46.4 1.0 CA A:HIS248 4.7 47.9 1.0 C A:HIS248 4.7 49.4 1.0 ND1 A:HIS248 4.8 60.4 1.0 OD1 A:ASN124 4.8 43.4 1.0 CZ A:TYR272 5.0 61.6 1.0

Manganese binding site 2 out of 4 in the The KNL1-PP1 Holoenzyme


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of The KNL1-PP1 Holoenzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn402 b:47.7 occ:1.00 O4 A:PO4403 2.1 44.5 1.0 OD2 A:ASP92 2.2 61.3 1.0 NE2 A:HIS173 2.2 39.3 1.0 OD1 A:ASN124 2.2 43.4 1.0 O A:HOH501 2.2 73.8 1.0 ND1 A:HIS248 2.2 60.4 1.0 CE1 A:HIS248 2.9 57.3 1.0 CE1 A:HIS173 3.0 41.5 1.0 CG A:ASP92 3.1 48.0 1.0 MN A:MN401 3.1 57.3 1.0 CG A:ASN124 3.2 46.6 1.0 CD2 A:HIS173 3.2 50.7 1.0 P A:PO4403 3.4 78.0 1.0 CG A:HIS248 3.4 51.6 1.0 OD1 A:ASP92 3.5 42.0 1.0 ND2 A:ASN124 3.6 40.5 1.0 CA A:HIS248 3.6 47.9 1.0 O1 A:PO4403 3.7 56.1 1.0 OD2 A:ASP64 3.9 50.9 1.0 CB A:HIS248 3.9 43.3 1.0 O A:HIS248 4.0 56.1 1.0 O3 A:PO4403 4.1 68.6 1.0 NE2 A:HIS248 4.1 51.4 1.0 ND1 A:HIS173 4.2 45.8 1.0 CD2 A:HIS125 4.3 42.7 1.0 C A:HIS248 4.3 49.4 1.0 CG A:HIS173 4.3 48.8 1.0 CD2 A:HIS248 4.4 39.7 1.0 CB A:ASP92 4.4 46.7 1.0 CB A:ASN124 4.5 37.6 1.0 O A:HOH510 4.5 64.7 1.0 O2 A:PO4403 4.5 49.2 1.0 N A:ASN124 4.6 38.6 1.0 N A:HIS248 4.6 53.3 1.0 O A:LEU205 4.8 54.1 1.0 CG A:ASP64 4.8 62.4 1.0 NE2 A:HIS66 5.0 56.9 1.0

Manganese binding site 3 out of 4 in the The KNL1-PP1 Holoenzyme


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of The KNL1-PP1 Holoenzyme within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn401 b:63.0 occ:1.00 OD2 C:ASP64 2.1 50.8 1.0 OD2 C:ASP92 2.2 70.3 1.0 O C:HOH502 2.2 79.0 1.0 O C:HOH510 2.2 67.5 1.0 NE2 C:HIS66 2.2 70.2 1.0 O2 C:PO4403 2.4 72.0 1.0 MN C:MN402 3.0 48.0 1.0 CE1 C:HIS66 3.1 53.7 1.0 CG C:ASP92 3.1 58.5 1.0 O3 C:PO4403 3.2 50.5 1.0 P C:PO4403 3.2 94.5 1.0 CG C:ASP64 3.3 57.3 1.0 CD2 C:HIS66 3.3 52.6 1.0 CB C:ASP92 3.6 46.9 1.0 O4 C:PO4403 3.7 96.0 1.0 CD2 C:HIS125 4.0 59.8 1.0 CB C:ASP64 4.1 48.8 1.0 OD1 C:ASP92 4.2 52.4 1.0 OD1 C:ASP64 4.2 59.0 1.0 ND1 C:HIS66 4.2 51.8 1.0 CE1 C:HIS173 4.4 44.0 1.0 NE2 C:HIS173 4.4 43.5 1.0 O C:HIS248 4.4 67.1 1.0 CG C:HIS66 4.4 52.1 1.0 NE2 C:HIS125 4.4 75.5 1.0 OH C:TYR272 4.4 87.4 1.0 O1 C:PO4403 4.6 69.8 1.0 CE1 C:PHE267 4.7 53.0 1.0 CA C:HIS248 4.7 60.4 1.0 ND1 C:HIS248 4.7 74.1 1.0 C C:HIS248 4.8 61.2 1.0 OD1 C:ASN124 4.8 45.7 1.0

Manganese binding site 4 out of 4 in the The KNL1-PP1 Holoenzyme


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of The KNL1-PP1 Holoenzyme within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn402 b:48.0 occ:1.00 NE2 C:HIS173 2.2 43.5 1.0 OD1 C:ASN124 2.2 45.7 1.0 OD2 C:ASP92 2.2 70.3 1.0 O3 C:PO4403 2.2 50.5 1.0 O C:HOH502 2.2 79.0 1.0 ND1 C:HIS248 2.2 74.1 1.0 CE1 C:HIS248 2.8 68.7 1.0 CE1 C:HIS173 3.0 44.0 1.0 MN C:MN401 3.0 63.0 1.0 CG C:ASN124 3.1 51.9 1.0 CG C:ASP92 3.2 58.5 1.0 CD2 C:HIS173 3.2 46.7 1.0 CG C:HIS248 3.4 56.1 1.0 P C:PO4403 3.4 94.5 1.0 ND2 C:ASN124 3.5 36.2 1.0 OD1 C:ASP92 3.6 52.4 1.0 CA C:HIS248 3.7 60.4 1.0 O2 C:PO4403 3.9 72.0 1.0 O4 C:PO4403 3.9 96.0 1.0 O C:HIS248 4.0 67.1 1.0 OD2 C:ASP64 4.0 50.8 1.0 CB C:HIS248 4.0 52.8 1.0 NE2 C:HIS248 4.1 61.0 1.0 ND1 C:HIS173 4.2 43.6 1.0 CD2 C:HIS125 4.2 59.8 1.0 C C:HIS248 4.3 61.2 1.0 CG C:HIS173 4.3 46.3 1.0 CD2 C:HIS248 4.4 51.2 1.0 CB C:ASP92 4.5 46.9 1.0 CB C:ASN124 4.5 38.0 1.0 N C:ASN124 4.6 49.4 1.0 O1 C:PO4403 4.6 69.8 1.0 O C:HOH510 4.7 67.5 1.0 N C:HIS248 4.7 65.2 1.0 O C:LEU205 4.8 54.6 1.0 CG C:ASP64 4.9 57.3 1.0 NE2 C:HIS125 4.9 75.5 1.0 NE2 C:HIS66 5.0 70.2 1.0

R.Bajaj, M.Bollen, W.Peti, R.Page. KNL1 Binding to PP1 and Microtubules Is Mutually Exclusive. Structure V. 26 1327 2018.
ISSN: ISSN 1878-4186
PubMed: 30100357
DOI: 10.1016/J.STR.2018.06.013