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Potassium in PDB 3gai: Structure of A F112A Variant Pduo-Type Atp:Corrinoid Adenosyltransferase From Lactobacillus Reuteri Complexed with Cobalamin and Atp

Enzymatic activity of Structure of A F112A Variant Pduo-Type Atp:Corrinoid Adenosyltransferase From Lactobacillus Reuteri Complexed with Cobalamin and Atp

All present enzymatic activity of Structure of A F112A 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 F112A Variant Pduo-Type Atp:Corrinoid Adenosyltransferase From Lactobacillus Reuteri Complexed with Cobalamin and Atp, PDB code: 3gai 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 / 1.48
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 80.745, 80.745, 89.693, 90.00, 90.00, 120.00
R / Rfree (%) 15.6 / 17.4

Other elements in 3gai:

The structure of Structure of A F112A Variant Pduo-Type Atp:Corrinoid Adenosyltransferase From Lactobacillus Reuteri Complexed with Cobalamin and Atp also contains other interesting chemical elements:

Cobalt (Co) 1 atom
Magnesium (Mg) 1 atom
Chlorine (Cl) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Structure of A F112A Variant Pduo-Type Atp:Corrinoid Adenosyltransferase From Lactobacillus Reuteri Complexed with Cobalamin and Atp (pdb code 3gai). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Structure of A F112A Variant Pduo-Type Atp:Corrinoid Adenosyltransferase From Lactobacillus Reuteri Complexed with Cobalamin and Atp, PDB code: 3gai:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 3gai

Go back to Potassium Binding Sites List in 3gai
Potassium binding site 1 out of 2 in the Structure of A F112A 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 F112A 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:K190

b:15.8
occ:1.00
 O2A A:ATP999 2.7 13.4 1.0
OD2 A:ASP160 2.7 16.7 1.0
OD1 A:ASP160 2.7 15.8 1.0
O2G A:ATP999 2.8 13.1 1.0
O1G A:ATP999 2.9 14.7 1.0
CG A:ASP160 3.1 16.1 1.0
PG A:ATP999 3.3 13.6 1.0
O1A A:ATP999 3.4 12.8 1.0
PA A:ATP999 3.5 13.6 1.0
C35 A:B12800 3.5 14.8 1.0
O A:HOH203 3.8 13.1 1.0
N29 A:B12800 4.0 16.5 1.0
MG A:MG189 4.0 12.9 1.0
O A:HOH202 4.0 16.3 1.0
O3B A:ATP999 4.0 12.5 1.0
O3A A:ATP999 4.4 13.0 1.0
C5 A:B12800 4.5 14.5 1.0
CB A:ASP160 4.5 12.9 1.0
C37 A:B12800 4.7 13.0 1.0
O3G A:ATP999 4.7 13.8 1.0
PB A:ATP999 4.8 13.2 1.0
O5' A:ATP999 4.8 12.2 1.0
N40 A:B12800 4.9 13.9 1.0
O1B A:ATP999 4.9 12.8 1.0

Potassium binding site 2 out of 2 in 3gai

Go back to Potassium Binding Sites List in 3gai
Potassium binding site 2 out of 2 in the Structure of A F112A 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 2 of Structure of A F112A 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:21.6
occ:1.00
 O A:HIS82 2.5 21.6 1.0
O A:HOH264 2.6 28.2 1.0
O A:ASP79 2.7 19.9 1.0
O A:PRO76 2.8 18.8 1.0
O A:HOH260 2.8 32.2 1.0
O A:ALA77 2.9 22.4 1.0
C A:ALA77 3.4 21.2 1.0
C A:ASP79 3.5 19.7 1.0
C A:HIS82 3.7 20.5 1.0
CA A:ALA77 3.8 20.0 1.0
C A:PRO76 3.9 18.0 1.0
N A:ASP79 3.9 21.1 1.0
CG2 A:THR75 4.0 20.0 1.0
CA A:ASP79 4.2 19.9 1.0
N A:GLU80 4.3 19.9 1.0
N A:ALA77 4.3 18.5 1.0
N A:ASP78 4.3 21.7 1.0
CA A:GLU80 4.4 21.1 1.0
C A:ASP78 4.6 22.4 1.0
CA A:HIS82 4.6 20.3 1.0
N A:HIS82 4.6 19.4 1.0
N A:SER83 4.7 20.7 1.0
CA A:SER83 4.7 21.3 1.0
CB A:HIS82 4.7 20.5 1.0
CB A:ASP79 4.7 19.8 1.0
O A:HOH256 4.8 28.6 1.0
O A:HOH295 4.9 40.0 1.0
C A:GLU80 4.9 19.8 1.0
CA A:ASP78 5.0 22.5 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 08:22:32 2024

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