Potassium in PDB 7ruu: Structure of Human Atp:Cobalamin Adenosyltransferase R190C Bound to Adenosylcobalamin

Enzymatic activity of Structure of Human Atp:Cobalamin Adenosyltransferase R190C Bound to Adenosylcobalamin

All present enzymatic activity of Structure of Human Atp:Cobalamin Adenosyltransferase R190C Bound to Adenosylcobalamin:
2.5.1.17;

Protein crystallography data

The structure of Structure of Human Atp:Cobalamin Adenosyltransferase R190C Bound to Adenosylcobalamin, PDB code: 7ruu was solved by R.Mascarenhas, H.Gouda, M.Koutmos, R.Banerjee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.16 / 1.85
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 121.807, 121.807, 171.629, 90, 90, 120
R / Rfree (%) 17.7 / 20.2

Other elements in 7ruu:

The structure of Structure of Human Atp:Cobalamin Adenosyltransferase R190C Bound to Adenosylcobalamin also contains other interesting chemical elements:

Cobalt (Co) 4 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Structure of Human Atp:Cobalamin Adenosyltransferase R190C Bound to Adenosylcobalamin (pdb code 7ruu). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 3 binding sites of Potassium where determined in the Structure of Human Atp:Cobalamin Adenosyltransferase R190C Bound to Adenosylcobalamin, PDB code: 7ruu:
Jump to Potassium binding site number: 1; 2; 3;

Potassium binding site 1 out of 3 in 7ruu

Go back to Potassium Binding Sites List in 7ruu
Potassium binding site 1 out of 3 in the Structure of Human Atp:Cobalamin Adenosyltransferase R190C Bound to Adenosylcobalamin


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of Human Atp:Cobalamin Adenosyltransferase R190C Bound to Adenosylcobalamin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K302

b:37.5
occ:0.33
 O A:HOH422 3.2 32.2 1.0
NH1 A:ARG195 3.4 34.7 1.0
CD A:ARG191 4.0 27.0 1.0
NH2 A:ARG191 4.4 24.9 1.0
OE2 A:GLU84 4.5 40.8 1.0
CZ A:ARG195 4.6 31.4 1.0
NE A:ARG191 4.6 26.0 1.0
CZ A:ARG191 4.8 28.2 1.0
NE A:ARG195 4.8 30.8 1.0

Potassium binding site 2 out of 3 in 7ruu

Go back to Potassium Binding Sites List in 7ruu
Potassium binding site 2 out of 3 in the Structure of Human Atp:Cobalamin Adenosyltransferase R190C Bound to Adenosylcobalamin


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Structure of Human Atp:Cobalamin Adenosyltransferase R190C Bound to Adenosylcobalamin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K303

b:42.0
occ:0.33
 NZ A:LYS177 3.0 54.8 1.0
CE A:LYS177 3.7 54.2 1.0
CZ A:PHE98 4.2 29.1 1.0
CD A:LYS177 4.4 52.3 1.0
CD2 A:LEU102 4.4 32.0 1.0
O A:HOH404 4.7 63.6 1.0
CE2 A:PHE98 5.0 29.8 1.0

Potassium binding site 3 out of 3 in 7ruu

Go back to Potassium Binding Sites List in 7ruu
Potassium binding site 3 out of 3 in the Structure of Human Atp:Cobalamin Adenosyltransferase R190C Bound to Adenosylcobalamin


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Structure of Human Atp:Cobalamin Adenosyltransferase R190C Bound to Adenosylcobalamin within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K302

b:41.2
occ:1.00
 NH1 C:ARG195 3.2 39.0 1.0
O D:HOH427 3.2 39.8 1.0
NH1 D:ARG195 3.4 37.2 1.0
O C:HOH430 3.5 36.3 1.0
CD C:ARG191 4.0 31.5 1.0
CD D:ARG191 4.1 28.9 1.0
NH2 D:ARG191 4.3 28.9 1.0
NH2 C:ARG191 4.4 28.3 1.0
CZ C:ARG195 4.4 36.4 1.0
CZ D:ARG195 4.5 43.5 1.0
OE2 D:GLU84 4.5 39.0 1.0
OXT D:ACT304 4.5 65.0 1.0
OE2 C:GLU84 4.5 40.3 1.0
NE C:ARG191 4.6 31.1 1.0
NE D:ARG191 4.7 28.5 1.0
NE C:ARG195 4.7 37.2 1.0
NE D:ARG195 4.7 37.0 1.0
CZ D:ARG191 4.8 29.9 1.0
CZ C:ARG191 4.8 31.6 1.0
CH3 D:ACT304 4.8 56.2 1.0

Reference:

H.Gouda, R.Mascarenhas, S.Pillay, M.Ruetz, M.Koutmos, R.Banerjee. Patient Mutations in Human Atp:Cob(I)Alamin Adenosyltransferase Differentially Affect Its Catalytic Versus Chaperone Functions. J.Biol.Chem. 01373 2021.
ISSN: ESSN 1083-351X
PubMed: 34757128
DOI: 10.1016/J.JBC.2021.101373
Page generated: Mon Aug 12 20:56:39 2024

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