Cobalt in PDB 5eje: Crystal Structure of E. Coli Adenylate Kinase G56C/T163C Double Mutant in Complex with AP5A

All present enzymatic activity of Crystal Structure of E. Coli Adenylate Kinase G56C/T163C Double Mutant in Complex with AP5A:
2.7.4.3;

The structure of Crystal Structure of E. Coli Adenylate Kinase G56C/T163C Double Mutant in Complex with AP5A, PDB code: 5eje was solved by U.H.Sauer, M.Kovermann, C.Grundstrom, M.Wolf-Watz, A.E.Sauer-Eriksson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	26.80 / 1.90
Space group	P 21 2 21
Cell size a, b, c (Å), α, β, γ (°)	73.003, 79.064, 81.834, 90.00, 90.00, 90.00
R / Rfree (%)	18.6 / 23.6

The binding sites of Cobalt atom in the Crystal Structure of E. Coli Adenylate Kinase G56C/T163C Double Mutant in Complex with AP5A (pdb code 5eje). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Crystal Structure of E. Coli Adenylate Kinase G56C/T163C Double Mutant in Complex with AP5A, PDB code: 5eje:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the Crystal Structure of E. Coli Adenylate Kinase G56C/T163C Double Mutant in Complex with AP5A


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Crystal Structure of E. Coli Adenylate Kinase G56C/T163C Double Mutant in Complex with AP5A within 5.0Å range: probe atom residue distance (Å) B Occ A:Co302 b:27.6 occ:1.00 O1G A:AP5301 1.9 32.1 1.0 O2B A:AP5301 2.0 20.9 1.0 O A:HOH458 2.1 22.9 1.0 O A:HOH454 2.2 24.3 1.0 O A:HOH402 2.3 26.0 1.0 O A:HOH428 2.4 27.8 1.0 PG A:AP5301 3.2 30.8 1.0 PB A:AP5301 3.3 21.1 1.0 H A:GLY14 3.6 25.0 1.0 O3B A:AP5301 3.6 26.2 1.0 HA3 A:GLY14 3.7 30.8 1.0 HH12 A:ARG156 3.9 39.6 1.0 O2A A:AP5301 3.9 23.0 1.0 O A:HOH421 4.0 33.6 1.0 O3G A:AP5301 4.1 29.6 1.0 OD1 A:ASP84 4.2 27.5 1.0 OD2 A:ASP84 4.2 29.8 1.0 N A:GLY14 4.2 20.8 1.0 O1E A:AP5301 4.3 23.5 1.0 O2E A:AP5301 4.3 23.3 1.0 O3A A:AP5301 4.3 24.4 1.0 HH12 A:ARG123 4.3 30.9 1.0 O2G A:AP5301 4.4 30.9 1.0 CA A:GLY14 4.4 25.7 1.0 O3D A:AP5301 4.4 26.8 1.0 HH11 A:ARG156 4.4 39.6 1.0 O1B A:AP5301 4.4 19.4 1.0 HH22 A:ARG36 4.5 33.0 1.0 NH1 A:ARG156 4.5 33.0 1.0 HB2 A:LYS13 4.5 22.9 1.0 PE A:AP5301 4.5 24.2 1.0 PA A:AP5301 4.5 22.5 1.0 HG A:SER30 4.5 34.7 1.0 O A:HOH485 4.5 42.5 1.0 HA2 A:GLY14 4.6 30.8 1.0 HE2 A:LYS13 4.6 27.5 1.0 CG A:ASP84 4.6 26.9 1.0 HH11 A:ARG123 4.7 30.9 1.0 NH1 A:ARG123 4.7 25.7 1.0 HG11 A:VAL132 4.8 40.0 1.0 O1A A:AP5301 4.8 19.8 1.0 OG A:SER30 4.9 28.9 1.0 O A:HOH441 4.9 28.5 1.0

Cobalt binding site 2 out of 2 in the Crystal Structure of E. Coli Adenylate Kinase G56C/T163C Double Mutant in Complex with AP5A


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Crystal Structure of E. Coli Adenylate Kinase G56C/T163C Double Mutant in Complex with AP5A within 5.0Å range: probe atom residue distance (Å) B Occ B:Co302 b:29.1 occ:1.00 O1G B:AP5301 1.8 35.9 1.0 O B:HOH402 2.0 27.4 1.0 O B:HOH466 2.0 28.2 1.0 O B:HOH442 2.1 27.3 1.0 O2B B:AP5301 2.1 25.2 1.0 O B:HOH462 2.2 25.1 1.0 PG B:AP5301 3.1 33.5 1.0 PB B:AP5301 3.3 22.6 1.0 H B:GLY14 3.6 33.8 1.0 O3B B:AP5301 3.6 27.3 1.0 HA3 B:GLY14 3.7 31.4 1.0 HH12 B:ARG156 3.8 46.7 1.0 O2A B:AP5301 4.0 23.2 1.0 O3G B:AP5301 4.1 31.1 1.0 O3D B:AP5301 4.2 31.1 1.0 N B:GLY14 4.2 28.2 1.0 O2E B:AP5301 4.2 26.8 1.0 O B:HOH430 4.3 33.9 1.0 O2G B:AP5301 4.3 37.2 1.0 OD1 B:ASP84 4.3 32.2 1.0 OD2 B:ASP84 4.3 31.9 1.0 O1E B:AP5301 4.3 29.4 1.0 HH12 B:ARG123 4.3 43.2 1.0 CA B:GLY14 4.4 26.2 1.0 O3A B:AP5301 4.4 22.5 1.0 O1B B:AP5301 4.4 18.9 1.0 PE B:AP5301 4.4 24.3 1.0 NH1 B:ARG156 4.4 38.9 1.0 HH11 B:ARG156 4.5 46.7 1.0 HB2 B:LYS13 4.5 30.4 1.0 HG B:SER30 4.5 45.1 1.0 PA B:AP5301 4.5 23.0 1.0 HH22 B:ARG36 4.6 39.2 1.0 HH11 B:ARG123 4.6 43.2 1.0 HE2 B:LYS13 4.6 31.6 1.0 O B:HOH501 4.6 38.9 1.0 HA2 B:GLY14 4.6 31.4 1.0 CG B:ASP84 4.7 31.4 1.0 NH1 B:ARG123 4.7 36.0 1.0 O1A B:AP5301 4.8 24.9 1.0 O B:HOH441 4.9 31.3 1.0 PD B:AP5301 4.9 32.9 1.0 OG B:SER30 5.0 37.6 1.0

M.Kovermann, C.Grundstrom, A.E.Sauer-Eriksson, U.H.Sauer, M.Wolf-Watz. Structural Basis For Ligand Binding to An Enzyme By A Conformational Selection Pathway. Proc. Natl. Acad. Sci. V. 114 6298 2017U.S.A..
ISSN: ESSN 1091-6490
PubMed: 28559350
DOI: 10.1073/PNAS.1700919114