Potassium in PDB 1n31: Structure of A Catalytically Inactive Mutant (K223A) of C-Des with A Substrate (Cystine) Linked to the Co-Factor

The structure of Structure of A Catalytically Inactive Mutant (K223A) of C-Des with A Substrate (Cystine) Linked to the Co-Factor, PDB code: 1n31 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)	19.92 / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	62.681, 65.843, 172.563, 90.00, 90.00, 90.00
R / Rfree (%)	19.6 / 25.6

The binding sites of Potassium atom in the Structure of A Catalytically Inactive Mutant (K223A) of C-Des with A Substrate (Cystine) Linked to the Co-Factor (pdb code 1n31). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Structure of A Catalytically Inactive Mutant (K223A) of C-Des with A Substrate (Cystine) Linked to the Co-Factor, PDB code: 1n31:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Structure of A Catalytically Inactive Mutant (K223A) of C-Des with A Substrate (Cystine) Linked to the Co-Factor


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of A Catalytically Inactive Mutant (K223A) of C-Des with A Substrate (Cystine) Linked to the Co-Factor within 5.0Å range: probe atom residue distance (Å) B Occ A:K1001 b:35.2 occ:1.00 O A:LEU319 2.5 38.2 1.0 O A:VAL322 2.6 36.6 1.0 O A:ASN317 2.9 35.3 1.0 O A:LEU316 3.1 27.0 1.0 O A:HOH3190 3.4 35.6 1.0 C A:ASN317 3.4 34.6 1.0 O A:HOH3028 3.5 31.4 1.0 C A:LEU319 3.6 36.2 1.0 CA A:ASN317 3.6 33.0 1.0 C A:VAL322 3.7 36.2 1.0 C A:LEU316 4.1 29.5 1.0 N A:LEU319 4.2 38.3 1.0 O A:HOH3137 4.3 29.0 1.0 N A:VAL322 4.4 35.6 1.0 N A:ASN317 4.4 30.8 1.0 N A:GLN318 4.4 35.9 1.0 CA A:LEU319 4.5 37.3 1.0 N A:PRO320 4.5 35.9 1.0 CD2 A:HIS323 4.5 44.2 1.0 CA A:VAL322 4.5 35.7 1.0 CA A:PRO320 4.5 36.3 1.0 O A:PRO320 4.5 34.1 1.0 C A:PRO320 4.6 35.6 1.0 C A:GLN318 4.6 38.4 1.0 CB A:VAL322 4.6 35.4 1.0 O A:HOH3223 4.6 59.9 1.0 N A:HIS323 4.7 35.8 1.0 CA A:HIS323 4.7 34.4 1.0 CB A:ASN317 4.8 32.4 1.0 CB A:LEU319 4.9 35.4 1.0 CA A:GLN318 5.0 37.7 1.0 NE2 A:HIS323 5.0 46.7 1.0

Potassium binding site 2 out of 2 in the Structure of A Catalytically Inactive Mutant (K223A) of C-Des with A Substrate (Cystine) Linked to the Co-Factor


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Structure of A Catalytically Inactive Mutant (K223A) of C-Des with A Substrate (Cystine) Linked to the Co-Factor within 5.0Å range: probe atom residue distance (Å) B Occ B:K1002 b:44.3 occ:1.00 O B:VAL322 2.4 35.0 1.0 O B:LEU319 2.6 38.9 1.0 O B:HOH3109 3.0 31.6 1.0 O B:ASN317 3.0 38.1 1.0 O B:LEU316 3.2 28.2 1.0 C B:ASN317 3.5 37.5 1.0 C B:VAL322 3.6 34.9 1.0 O B:HOH3136 3.7 36.0 1.0 CA B:ASN317 3.7 36.0 1.0 C B:LEU319 3.7 37.0 1.0 C B:LEU316 4.1 30.1 1.0 N B:VAL322 4.3 34.6 1.0 N B:LEU319 4.4 38.4 1.0 CA B:VAL322 4.4 34.0 1.0 CD2 B:HIS323 4.4 44.6 1.0 N B:ASN317 4.4 33.8 1.0 N B:HIS323 4.5 35.0 1.0 N B:GLN318 4.5 38.2 1.0 CB B:VAL322 4.5 34.2 1.0 N B:PRO320 4.6 37.0 1.0 CA B:LEU319 4.6 37.1 1.0 O B:PRO320 4.6 35.7 1.0 CA B:HIS323 4.6 34.7 1.0 C B:PRO320 4.6 36.1 1.0 CA B:PRO320 4.6 37.3 1.0 C B:GLN318 4.7 40.1 1.0 CB B:ASN317 4.9 34.8 1.0 NE2 B:HIS323 4.9 48.0 1.0 CG B:HIS323 5.0 44.2 1.0 CB B:LEU319 5.0 36.0 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