Potassium in PDB 1n2t: C-Des Mutant K223A with Gly Covalenty Linked to the Plp-Cofactor

The structure of C-Des Mutant K223A with Gly Covalenty Linked to the Plp-Cofactor, PDB code: 1n2t was solved by J.T.Kaiser, S.Bruno, T.Clausen, R.Huber, F.Schiaretti, A.Mozzarelli, D.Kessler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.95 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	62.752, 66.237, 172.792, 90.00, 90.00, 90.00
R / Rfree (%)	20.1 / 24.5

The binding sites of Potassium atom in the C-Des Mutant K223A with Gly Covalenty Linked to the Plp-Cofactor (pdb code 1n2t). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the C-Des Mutant K223A with Gly Covalenty Linked to the Plp-Cofactor, PDB code: 1n2t:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the C-Des Mutant K223A with Gly Covalenty Linked to the Plp-Cofactor


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of C-Des Mutant K223A with Gly Covalenty Linked to the Plp-Cofactor within 5.0Å range: probe atom residue distance (Å) B Occ A:K1001 b:34.8 occ:1.00 O A:LEU319 2.5 38.4 1.0 O A:VAL322 2.6 31.7 1.0 O A:ASN317 2.9 33.2 1.0 O A:LEU316 3.1 26.3 1.0 C A:ASN317 3.3 34.8 1.0 O A:HOH3085 3.4 31.1 1.0 CA A:ASN317 3.6 33.8 1.0 C A:LEU319 3.6 37.2 1.0 C A:VAL322 3.8 32.3 1.0 O A:HOH3201 4.1 31.2 1.0 C A:LEU316 4.1 28.6 1.0 N A:LEU319 4.1 37.6 1.0 N A:GLN318 4.3 37.4 1.0 N A:ASN317 4.3 29.9 1.0 CA A:LEU319 4.4 37.2 1.0 C A:GLN318 4.5 39.0 1.0 N A:PRO320 4.5 37.0 1.0 N A:VAL322 4.5 32.9 1.0 CA A:VAL322 4.6 32.2 1.0 CD2 A:HIS323 4.6 43.9 1.0 CA A:PRO320 4.7 36.7 1.0 O A:PRO320 4.7 36.7 1.0 N A:HIS323 4.7 31.7 1.0 C A:PRO320 4.7 36.5 1.0 CA A:HIS323 4.7 32.2 1.0 CB A:VAL322 4.7 28.7 1.0 CB A:ASN317 4.8 32.1 1.0 CA A:GLN318 4.9 39.4 1.0 O A:HOH3276 4.9 40.4 1.0 CB A:LEU319 5.0 34.2 1.0

Potassium binding site 2 out of 2 in the C-Des Mutant K223A with Gly Covalenty Linked to the Plp-Cofactor


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of C-Des Mutant K223A with Gly Covalenty Linked to the Plp-Cofactor within 5.0Å range: probe atom residue distance (Å) B Occ B:K1002 b:42.3 occ:1.00 O B:VAL322 2.4 33.0 1.0 O B:LEU319 2.6 40.3 1.0 O B:HOH2204 3.1 32.3 1.0 O B:ASN317 3.1 35.8 1.0 O B:LEU316 3.4 28.3 1.0 C B:VAL322 3.6 31.8 1.0 O B:HOH2167 3.6 37.4 1.0 C B:ASN317 3.7 35.8 1.0 C B:LEU319 3.8 39.1 1.0 CA B:ASN317 3.8 33.3 1.0 CD2 B:HIS323 4.3 43.5 1.0 C B:LEU316 4.4 26.9 1.0 N B:VAL322 4.4 34.2 1.0 N B:LEU319 4.5 40.6 1.0 CA B:HIS323 4.5 31.3 1.0 N B:HIS323 4.5 32.7 1.0 CA B:VAL322 4.5 31.4 1.0 O B:PRO320 4.5 38.4 1.0 N B:ASN317 4.6 29.8 1.0 C B:PRO320 4.6 36.5 1.0 N B:PRO320 4.6 39.4 1.0 N B:GLN318 4.6 35.9 1.0 CA B:PRO320 4.6 36.8 1.0 CA B:LEU319 4.7 39.4 1.0 CB B:VAL322 4.7 30.3 1.0 C B:GLN318 4.8 40.9 1.0 NE2 B:HIS323 4.9 45.0 1.0 CG B:HIS323 4.9 42.0 1.0

J.T.Kaiser, S.Bruno, T.Clausen, R.Huber, F.Schiaretti, A.Mozzarelli, D.Kessler. Snapshots of the Cystine Lyase "C-Des" During Catalysis: Studies in Solution and in the Crystalline State J.Biol.Chem. V. 278 357 2003.
ISSN: ISSN 0021-9258
PubMed: 12386155
DOI: 10.1074/JBC.M209862200