Potassium in PDB 1ope: Deletion Mutant of Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart

All present enzymatic activity of Deletion Mutant of Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart:
2.8.3.5;

The structure of Deletion Mutant of Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart, PDB code: 1ope was solved by A.M.Coros, L.Swenson, W.T.Wolodko, M.E.Fraser, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.13 / 2.50
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	147.640, 68.700, 103.500, 90.00, 99.58, 90.00
R / Rfree (%)	18 / 23.5

The structure of Deletion Mutant of Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart also contains other interesting chemical elements:

Mercury

(Hg)

4 atoms

The binding sites of Potassium atom in the Deletion Mutant of Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart (pdb code 1ope). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Deletion Mutant of Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart, PDB code: 1ope:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Deletion Mutant of Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Deletion Mutant of Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart within 5.0Å range: probe atom residue distance (Å) B Occ A:K484 b:45.0 occ:1.00 O A:THR396 2.5 21.8 1.0 O A:HOH537 2.7 30.7 1.0 OD1 A:ASN428 2.8 19.6 1.0 O A:SER393 3.2 24.1 1.0 C A:THR396 3.6 21.6 1.0 CG A:ASN428 3.7 22.7 1.0 ND2 A:ASN428 3.8 24.3 1.0 O A:ALA394 3.9 29.3 1.0 O A:CYS426 3.9 38.7 1.0 CA A:ALA394 4.0 26.4 1.0 CG2 A:VAL398 4.0 9.2 1.0 C A:ALA394 4.1 26.9 1.0 C A:SER393 4.2 24.8 1.0 N A:VAL398 4.3 16.7 1.0 N A:THR396 4.3 25.0 1.0 CA A:LYS397 4.4 18.5 1.0 N A:LYS397 4.4 19.3 1.0 CA A:THR396 4.5 22.3 1.0 N A:ALA394 4.6 26.4 1.0 CB A:VAL398 4.6 17.0 1.0 C A:LYS397 4.7 19.3 1.0 C A:CYS426 4.8 37.8 1.0

Potassium binding site 2 out of 2 in the Deletion Mutant of Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Deletion Mutant of Succinyl-Coa:3-Ketoacid Coa Transferase From Pig Heart within 5.0Å range: probe atom residue distance (Å) B Occ B:K484 b:42.6 occ:1.00 O B:THR396 2.5 14.8 1.0 OD1 B:ASN428 2.7 15.1 1.0 O B:SER393 3.3 22.3 1.0 CG B:ASN428 3.6 17.6 1.0 O B:CYS426 3.6 21.6 1.0 C B:THR396 3.7 16.1 1.0 ND2 B:ASN428 3.8 17.4 1.0 CG2 B:VAL398 3.8 13.5 1.0 N B:VAL398 4.1 15.0 1.0 O B:ALA394 4.1 22.1 1.0 CA B:ALA394 4.2 20.8 1.0 CA B:LYS397 4.4 16.6 1.0 C B:SER393 4.4 21.8 1.0 C B:ALA394 4.4 21.9 1.0 CB B:VAL398 4.4 15.8 1.0 N B:LYS397 4.5 15.4 1.0 N B:THR396 4.5 19.9 1.0 C B:CYS426 4.5 23.8 1.0 C B:LYS397 4.6 16.5 1.0 CA B:THR396 4.6 17.8 1.0 N B:ALA394 4.8 22.0 1.0 CA B:VAL398 4.9 15.1 1.0 CA B:CYS426 4.9 24.7 1.0

A.M.Coros, L.Swenson, W.T.Wolodko, M.E.Fraser. Structure of the Coa Transferase From Pig Heart to 1.7 A Resolution. Acta Crystallogr.,Sect.D V. 60 1717 2004.
ISSN: ISSN 0907-4449
PubMed: 15388917
DOI: 10.1107/S0907444904017974