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Cobalt in PDB 5ng0: Structure of RIP2K(L294F) with Bound Amppcp

Enzymatic activity of Structure of RIP2K(L294F) with Bound Amppcp

All present enzymatic activity of Structure of RIP2K(L294F) with Bound Amppcp:
2.7.10.2; 2.7.11.1;

Protein crystallography data

The structure of Structure of RIP2K(L294F) with Bound Amppcp, PDB code: 5ng0 was solved by E.Pellegrini, S.Cusack, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.00
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 94.180, 94.180, 201.250, 90.00, 90.00, 90.00
R / Rfree (%) 17 / 19.1

Other elements in 5ng0:

The structure of Structure of RIP2K(L294F) with Bound Amppcp also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Structure of RIP2K(L294F) with Bound Amppcp (pdb code 5ng0). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the Structure of RIP2K(L294F) with Bound Amppcp, PDB code: 5ng0:

Cobalt binding site 1 out of 1 in 5ng0

Go back to Cobalt Binding Sites List in 5ng0
Cobalt binding site 1 out of 1 in the Structure of RIP2K(L294F) with Bound Amppcp


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Structure of RIP2K(L294F) with Bound Amppcp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Co403

b:0.4
occ:1.00
CE2 B:TRP170 3.9 33.6 1.0
NZ B:LYS72 3.9 45.0 1.0
NE1 B:TRP170 4.1 33.6 1.0
CD2 B:TRP170 4.1 32.0 1.0
CZ2 B:TRP170 4.2 33.2 1.0
CD1 B:TRP170 4.4 35.5 1.0
CD B:PRO140 4.4 33.1 1.0
CG B:TRP170 4.4 32.5 1.0
CE B:LYS72 4.4 37.0 1.0
CD B:LYS72 4.5 35.7 1.0
CE3 B:TRP170 4.6 32.9 1.0
O B:HOH621 4.6 54.4 1.0
CH2 B:TRP170 4.6 33.2 1.0
CG B:PRO140 4.7 33.7 1.0
CZ3 B:TRP170 4.8 32.1 1.0

Reference:

E.Pellegrini, L.Signor, S.Singh, E.Boeri Erba, S.Cusack. Structures of the Inactive and Active States of RIP2 Kinase Inform on the Mechanism of Activation. Plos One V. 12 77161 2017.
ISSN: ESSN 1932-6203
PubMed: 28545134
DOI: 10.1371/JOURNAL.PONE.0177161
Page generated: Tue Jul 30 18:08:44 2024

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