Potassium in PDB 1ooz: 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: 1ooz 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)	39.73 / 2.10
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	96.819, 139.112, 68.476, 90.00, 90.00, 90.00
R / Rfree (%)	16.1 / 21

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

Potassium binding site 1 out of 3 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:K482 b:24.6 occ:1.00 O A:THR396 2.5 13.8 1.0 O A:HOH599 2.5 32.9 1.0 OD1 A:ASN428 2.8 12.3 1.0 O A:HOH840 2.8 34.4 1.0 O A:SER393 3.3 11.3 1.0 O A:CYS426 3.3 18.7 1.0 CG A:ASN428 3.6 16.3 1.0 O A:HOH732 3.7 33.5 1.0 C A:THR396 3.7 13.3 1.0 O A:ALA394 3.8 18.4 1.0 ND2 A:ASN428 3.8 16.1 1.0 CG2 A:VAL398 3.8 7.3 1.0 N A:VAL398 4.0 9.5 1.0 CA A:ALA394 4.0 15.5 1.0 C A:ALA394 4.1 16.7 1.0 O A:HOH745 4.3 33.5 1.0 C A:CYS426 4.3 16.7 1.0 C A:SER393 4.3 11.2 1.0 CB A:VAL398 4.3 9.9 1.0 CA A:LYS397 4.4 12.6 1.0 N A:THR396 4.5 13.5 1.0 C A:LYS397 4.5 11.0 1.0 N A:LYS397 4.6 11.9 1.0 N A:ALA394 4.6 12.6 1.0 CA A:CYS426 4.7 17.0 1.0 CA A:THR396 4.7 12.8 1.0 CA A:VAL398 4.8 9.5 1.0 O A:HOH666 5.0 27.5 1.0

Potassium binding site 2 out of 3 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 A:K483 b:33.9 occ:1.00 O A:HOH777 2.6 28.3 1.0 O A:LYS424 2.7 14.1 1.0 O A:HOH680 2.8 24.7 1.0 O A:HOH732 3.1 33.5 1.0 O A:GLN425 3.1 15.2 1.0 O A:HOH738 3.2 45.0 1.0 O A:HOH637 3.6 35.4 1.0 C A:GLN425 3.7 16.3 1.0 C A:LYS424 3.9 15.3 1.0 CB A:CYS426 4.2 16.4 1.0 N A:CYS426 4.3 15.7 1.0 CA A:CYS426 4.3 17.0 1.0 O A:HOH524 4.3 16.0 1.0 CB A:GLN425 4.4 18.5 1.0 CA A:GLN425 4.5 16.9 1.0 O A:HOH577 4.5 17.7 1.0 N A:GLN425 4.7 15.2 1.0 O A:HOH523 4.9 12.7 1.0 CA A:LYS424 4.9 16.2 1.0 N A:LYS424 4.9 15.8 1.0

Potassium binding site 3 out of 3 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 3 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:K482 b:25.4 occ:1.00 O B:HOH577 2.5 31.4 1.0 O B:THR396 2.6 14.6 1.0 OD1 B:ASN428 2.7 8.2 1.0 O B:HOH666 2.8 27.3 1.0 O B:CYS426 3.1 16.9 1.0 O B:SER393 3.4 15.3 1.0 CG B:ASN428 3.6 11.3 1.0 CG2 B:VAL398 3.7 6.7 1.0 O B:HOH822 3.8 40.8 1.0 C B:THR396 3.9 13.1 1.0 ND2 B:ASN428 3.9 12.5 1.0 N B:VAL398 4.0 10.4 1.0 O B:ALA394 4.1 16.4 1.0 C B:CYS426 4.1 15.1 1.0 CA B:ALA394 4.1 14.7 1.0 CB B:VAL398 4.2 9.2 1.0 C B:ALA394 4.3 15.3 1.0 C B:SER393 4.4 15.8 1.0 CA B:LYS397 4.5 12.0 1.0 CA B:CYS426 4.5 16.3 1.0 C B:LYS397 4.6 11.5 1.0 N B:THR396 4.6 12.9 1.0 N B:LYS397 4.7 12.2 1.0 CA B:VAL398 4.7 9.2 1.0 N B:ALA394 4.7 14.6 1.0 CA B:THR396 4.8 14.2 1.0 O B:HOH606 5.0 34.5 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