Cobalt in PDB 3m59: SET7/9 Y245A in Complex with TAF10-K189ME2 Peptide and Adohcy

All present enzymatic activity of SET7/9 Y245A in Complex with TAF10-K189ME2 Peptide and Adohcy:
2.1.1.43;

The structure of SET7/9 Y245A in Complex with TAF10-K189ME2 Peptide and Adohcy, PDB code: 3m59 was solved by P.A.Del Rizzo, J.-F.Couture, M.S.Roiko, B.S.Strunk, J.S.Brunzelle, L.M.Dirk, R.L.Houtz, R.C.Trievel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.16 / 1.70
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	83.497, 83.497, 95.718, 90.00, 90.00, 120.00
R / Rfree (%)	18.7 / 20.6

The binding sites of Cobalt atom in the SET7/9 Y245A in Complex with TAF10-K189ME2 Peptide and Adohcy (pdb code 3m59). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 3 binding sites of Cobalt where determined in the SET7/9 Y245A in Complex with TAF10-K189ME2 Peptide and Adohcy, PDB code: 3m59:
Jump to Cobalt binding site number: 1; 2; 3;

Cobalt binding site 1 out of 3 in the SET7/9 Y245A in Complex with TAF10-K189ME2 Peptide and Adohcy


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of SET7/9 Y245A in Complex with TAF10-K189ME2 Peptide and Adohcy within 5.0Å range: probe atom residue distance (Å) B Occ A:Co367 b:59.8 occ:1.00 O A:HOH17 3.6 27.4 1.0 OG A:SER285 3.7 27.3 1.0 CB A:HIS283 4.0 24.7 1.0 N A:SER285 4.0 24.4 1.0 ND1 A:HIS283 4.1 33.1 1.0 CB A:SER285 4.1 25.4 1.0 N A:VAL284 4.3 22.5 1.0 CG A:HIS283 4.5 27.3 1.0 O A:HOH480 4.5 55.9 1.0 CA A:HIS283 4.5 24.1 1.0 C A:HIS283 4.6 22.1 1.0 CA A:SER285 4.7 25.2 1.0 C A:VAL284 4.9 24.1 1.0 CA A:VAL284 5.0 24.3 1.0

Cobalt binding site 2 out of 3 in the SET7/9 Y245A in Complex with TAF10-K189ME2 Peptide and Adohcy


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of SET7/9 Y245A in Complex with TAF10-K189ME2 Peptide and Adohcy within 5.0Å range: probe atom residue distance (Å) B Occ A:Co2 b:0.7 occ:1.00 N A:GLU351 3.4 40.4 1.0 N A:TRP352 3.5 39.3 1.0 CB A:GLU351 3.6 42.1 1.0 CD1 A:TRP352 3.8 34.1 1.0 CA A:GLU351 3.9 41.1 1.0 C A:GLU351 4.2 40.5 1.0 CB A:PRO350 4.3 38.8 1.0 C A:PRO350 4.3 39.6 1.0 CB A:TRP352 4.5 37.7 1.0 CG A:TRP352 4.5 36.0 1.0 CA A:TRP352 4.6 37.9 1.0 CA A:PRO350 4.6 38.8 1.0 CG A:GLU351 4.8 44.9 1.0 NE1 A:TRP352 4.8 32.4 1.0

Cobalt binding site 3 out of 3 in the SET7/9 Y245A in Complex with TAF10-K189ME2 Peptide and Adohcy


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 3 of SET7/9 Y245A in Complex with TAF10-K189ME2 Peptide and Adohcy within 5.0Å range: probe atom residue distance (Å) B Occ A:Co3 b:65.4 occ:1.00 O A:HOH83 3.5 45.9 1.0 OD1 A:ASN204 3.6 22.8 1.0 O A:HOH408 3.7 32.0 1.0 O A:HOH25 4.2 42.4 1.0 O A:HOH493 4.3 43.0 1.0 ND2 A:ASN204 4.4 19.2 1.0 CG A:ASN204 4.4 22.1 1.0 NE2 A:HIS192 4.7 34.0 1.0 CD2 A:HIS192 4.8 29.9 1.0

P.A.Del Rizzo, J.F.Couture, L.M.Dirk, B.S.Strunk, M.S.Roiko, J.S.Brunzelle, R.L.Houtz, R.C.Trievel. SET7/9 Catalytic Mutants Reveal the Role of Active Site Water Molecules in Lysine Multiple Methylation. J.Biol.Chem. V. 285 31849 2010.
ISSN: ISSN 0021-9258
PubMed: 20675860
DOI: 10.1074/JBC.M110.114587