Potassium in PDB 1zcz: Crystal Structure of Phosphoribosylaminoimidazolecarboxamide Formyltransferase / Imp Cyclohydrolase (TM1249) From Thermotoga Maritima at 1.88 A Resolution

The structure of Crystal Structure of Phosphoribosylaminoimidazolecarboxamide Formyltransferase / Imp Cyclohydrolase (TM1249) From Thermotoga Maritima at 1.88 A Resolution, PDB code: 1zcz was solved by Joint Center For Structural Genomics (Jcsg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.88
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	62.084, 58.630, 72.749, 99.26, 96.89, 106.13
R / Rfree (%)	15.6 / 19.7

The binding sites of Potassium atom in the Crystal Structure of Phosphoribosylaminoimidazolecarboxamide Formyltransferase / Imp Cyclohydrolase (TM1249) From Thermotoga Maritima at 1.88 A Resolution (pdb code 1zcz). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Crystal Structure of Phosphoribosylaminoimidazolecarboxamide Formyltransferase / Imp Cyclohydrolase (TM1249) From Thermotoga Maritima at 1.88 A Resolution, PDB code: 1zcz:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Crystal Structure of Phosphoribosylaminoimidazolecarboxamide Formyltransferase / Imp Cyclohydrolase (TM1249) From Thermotoga Maritima at 1.88 A Resolution


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of Phosphoribosylaminoimidazolecarboxamide Formyltransferase / Imp Cyclohydrolase (TM1249) From Thermotoga Maritima at 1.88 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:K453 b:34.0 occ:1.00 O A:ALA353 2.4 42.1 1.0 O A:VAL350 2.5 37.5 1.0 O A:VAL449 2.7 38.1 1.0 OD2 A:ASP399 2.7 43.8 1.0 O A:GLU351 2.8 42.2 1.0 C A:GLU351 3.3 38.6 1.0 CB A:ASP399 3.5 35.4 1.0 N A:ARG451 3.5 39.1 1.0 C A:ALA353 3.6 43.6 1.0 CG A:ASP399 3.6 38.1 1.0 CB A:ARG451 3.6 42.4 1.0 C A:VAL350 3.6 37.7 1.0 CA A:GLU351 3.8 37.7 1.0 OG A:SER355 3.9 36.4 1.0 N A:ALA353 3.9 41.7 1.0 C A:VAL449 3.9 38.8 1.0 C A:PHE450 3.9 40.2 1.0 CA A:ARG451 4.1 40.6 1.0 CA A:ALA353 4.2 40.6 1.0 N A:GLU351 4.2 35.5 1.0 N A:GLY352 4.2 39.7 1.0 CA A:PHE450 4.3 39.3 1.0 C A:GLY352 4.4 40.1 1.0 O A:ARG451 4.4 47.6 1.0 N A:PHE450 4.5 38.6 1.0 CB A:ALA353 4.6 41.3 1.0 O A:PHE450 4.6 39.9 1.0 N A:LYS354 4.7 42.6 1.0 CA A:GLY352 4.7 38.4 1.0 C A:ARG451 4.7 42.2 1.0 CG2 A:VAL449 4.7 39.5 1.0 CB A:ALA357 4.8 36.7 1.0 OD1 A:ASP399 4.8 39.0 1.0 N A:SER355 4.8 39.6 1.0 CB A:VAL449 4.9 35.7 1.0 C A:LYS354 4.9 41.3 1.0 CA A:VAL350 4.9 40.1 1.0 CG A:ARG451 4.9 41.0 1.0 CA A:LYS354 5.0 42.1 1.0 O A:GLY352 5.0 40.5 1.0

Potassium binding site 2 out of 2 in the Crystal Structure of Phosphoribosylaminoimidazolecarboxamide Formyltransferase / Imp Cyclohydrolase (TM1249) From Thermotoga Maritima at 1.88 A Resolution


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of Phosphoribosylaminoimidazolecarboxamide Formyltransferase / Imp Cyclohydrolase (TM1249) From Thermotoga Maritima at 1.88 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:K453 b:33.5 occ:1.00 O B:ALA353 2.5 40.8 1.0 O B:VAL350 2.5 36.1 1.0 O B:VAL449 2.7 37.0 1.0 OD2 B:ASP399 2.7 42.5 1.0 O B:GLU351 2.9 39.6 1.0 C B:GLU351 3.4 37.8 1.0 N B:ARG451 3.4 40.1 1.0 CB B:ARG451 3.6 39.9 1.0 CB B:ASP399 3.6 38.1 1.0 CG B:ASP399 3.6 38.9 1.0 C B:ALA353 3.6 41.0 1.0 C B:VAL350 3.6 36.8 1.0 CA B:GLU351 3.8 36.6 1.0 OG B:SER355 3.8 40.0 1.0 C B:VAL449 3.9 36.9 1.0 N B:ALA353 3.9 38.3 1.0 C B:PHE450 3.9 38.4 1.0 CA B:ARG451 4.0 40.5 1.0 N B:GLU351 4.1 37.2 1.0 CA B:PHE450 4.2 37.0 1.0 CA B:ALA353 4.2 37.8 1.0 N B:GLY352 4.2 39.8 1.0 C B:GLY352 4.4 40.2 1.0 O B:ARG451 4.5 43.0 1.0 N B:PHE450 4.5 36.3 1.0 O B:PHE450 4.6 38.6 1.0 CB B:ALA353 4.6 39.6 1.0 N B:LYS354 4.7 40.4 1.0 C B:ARG451 4.7 40.5 1.0 CA B:GLY352 4.7 39.5 1.0 CB B:ALA357 4.8 37.6 1.0 OD1 B:ASP399 4.8 36.9 1.0 CG2 B:VAL449 4.8 37.6 1.0 N B:SER355 4.8 41.4 1.0 C B:LYS354 4.9 42.8 1.0 CG B:ARG451 4.9 40.2 1.0 CB B:VAL449 4.9 34.4 1.0 CA B:VAL350 4.9 37.9 1.0

H.L.Axelrod, D.Mcmullan, S.S.Krishna, M.D.Miller, M.A.Elsliger, P.Abdubek, E.Ambing, T.Astakhova, D.Carlton, H.J.Chiu, T.Clayton, L.Duan, J.Feuerhelm, S.K.Grzechnik, J.Hale, G.W.Han, J.Haugen, L.Jaroszewski, K.K.Jin, H.E.Klock, M.W.Knuth, E.Koesema, A.T.Morse, E.Nigoghossian, L.Okach, S.Oommachen, J.Paulsen, K.Quijano, R.Reyes, C.L.Rife, H.Van Den Bedem, D.Weekes, A.White, G.Wolf, Q.Xu, K.O.Hodgson, J.Wooley, A.M.Deacon, A.Godzik, S.A.Lesley, I.A.Wilson. Crystal Structure of Aicar Transformylase Imp Cyclohydrolase (TM1249) From Thermotoga Maritima at 1.88 A Resolution. Proteins V. 71 1042 2008.
ISSN: ISSN 0887-3585
PubMed: 18260100
DOI: 10.1002/PROT.21967