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Potassium in PDB 3gah: Structure of A F112H Variant Pduo-Type Atp:Corrinoid Adenosyltransferase From Lactobacillus Reuteri Complexed with Cobalamin and Atp

Enzymatic activity of Structure of A F112H Variant Pduo-Type Atp:Corrinoid Adenosyltransferase From Lactobacillus Reuteri Complexed with Cobalamin and Atp

All present enzymatic activity of Structure of A F112H Variant Pduo-Type Atp:Corrinoid Adenosyltransferase From Lactobacillus Reuteri Complexed with Cobalamin and Atp:
2.5.1.17;

Protein crystallography data

The structure of Structure of A F112H Variant Pduo-Type Atp:Corrinoid Adenosyltransferase From Lactobacillus Reuteri Complexed with Cobalamin and Atp, PDB code: 3gah was solved by M.St Maurice, P.E.Mera, J.C.Escalante-Semerena, I.Rayment, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.17
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 80.814, 80.814, 89.492, 90.00, 90.00, 120.00
R / Rfree (%) 16 / 18.2

Other elements in 3gah:

The structure of Structure of A F112H Variant Pduo-Type Atp:Corrinoid Adenosyltransferase From Lactobacillus Reuteri Complexed with Cobalamin and Atp also contains other interesting chemical elements:

Cobalt (Co) 2 atoms
Magnesium (Mg) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Structure of A F112H Variant Pduo-Type Atp:Corrinoid Adenosyltransferase From Lactobacillus Reuteri Complexed with Cobalamin and Atp (pdb code 3gah). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Structure of A F112H Variant Pduo-Type Atp:Corrinoid Adenosyltransferase From Lactobacillus Reuteri Complexed with Cobalamin and Atp, PDB code: 3gah:

Potassium binding site 1 out of 1 in 3gah

Go back to Potassium Binding Sites List in 3gah
Potassium binding site 1 out of 1 in the Structure of A F112H Variant Pduo-Type Atp:Corrinoid Adenosyltransferase From Lactobacillus Reuteri Complexed with Cobalamin and Atp


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 F112H Variant Pduo-Type Atp:Corrinoid Adenosyltransferase From Lactobacillus Reuteri Complexed with Cobalamin and Atp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K191

b:10.2
occ:1.00
 O A:ILE3 2.6 12.6 1.0
O2A A:ATP999 2.7 10.1 1.0
O2G A:ATP999 2.8 8.8 1.0
O1G A:ATP999 2.8 10.7 1.0
PG A:ATP999 3.3 9.1 1.0
O1A A:ATP999 3.4 8.7 1.0
PA A:ATP999 3.5 8.6 1.0
C35 A:B12800 3.5 7.0 0.5
C35 A:B12800 3.6 17.2 0.5
C A:ILE3 3.7 11.9 1.0
O A:HOH193 3.8 8.9 1.0
O28 A:B12800 3.9 19.8 0.5
CA A:TYR4 4.0 11.1 1.0
MG A:MG189 4.0 8.5 1.0
O3B A:ATP999 4.0 9.7 1.0
O A:HOH194 4.0 11.5 1.0
O28 A:B12800 4.1 10.4 0.5
N A:TYR4 4.3 11.8 1.0
O3A A:ATP999 4.4 9.2 1.0
N A:THR5 4.4 11.8 1.0
C5 A:B12800 4.5 7.0 0.5
C37 A:B12800 4.6 7.5 0.5
C5 A:B12800 4.6 17.7 0.5
C37 A:B12800 4.6 14.1 0.5
O3G A:ATP999 4.7 10.2 1.0
C A:TYR4 4.8 12.5 1.0
PB A:ATP999 4.8 8.8 1.0
CA A:ILE3 4.8 13.1 1.0
N40 A:B12800 4.8 7.9 0.5
O5' A:ATP999 4.9 8.4 1.0
CB A:TYR4 4.9 11.0 1.0
CB A:ILE3 4.9 12.7 1.0

Reference:

P.E.Mera, M.St Maurice, I.Rayment, J.C.Escalante-Semerena. Residue PHE112 of the Human-Type Corrinoid Adenosyltransferase (Pduo) Enzyme of Lactobacillus Reuteri Is Critical to the Formation of the Four-Coordinate Co(II) Corrinoid Substrate and to the Activity of the Enzyme. Biochemistry V. 48 3138 2009.
ISSN: ISSN 0006-2960
PubMed: 19236001
DOI: 10.1021/BI9000134
Page generated: Mon Aug 12 08:22:07 2024

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