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Rubidium in PDB 8z5c: Cystal Structure of Beta-Ketoacyl-Acp Synthase Fabf From Helicobacter Pylori

Enzymatic activity of Cystal Structure of Beta-Ketoacyl-Acp Synthase Fabf From Helicobacter Pylori

All present enzymatic activity of Cystal Structure of Beta-Ketoacyl-Acp Synthase Fabf From Helicobacter Pylori:
2.3.1.179;

Protein crystallography data

The structure of Cystal Structure of Beta-Ketoacyl-Acp Synthase Fabf From Helicobacter Pylori, PDB code: 8z5c was solved by L.Zhang, Y.Z.Huang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.70 / 1.85
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 76.608, 95.382, 113.897, 90, 90, 90
R / Rfree (%) 15.8 / 19.3

Rubidium Binding Sites:

The binding sites of Rubidium atom in the Cystal Structure of Beta-Ketoacyl-Acp Synthase Fabf From Helicobacter Pylori (pdb code 8z5c). This binding sites where shown within 5.0 Angstroms radius around Rubidium atom.
In total 2 binding sites of Rubidium where determined in the Cystal Structure of Beta-Ketoacyl-Acp Synthase Fabf From Helicobacter Pylori, PDB code: 8z5c:
Jump to Rubidium binding site number: 1; 2;

Rubidium binding site 1 out of 2 in 8z5c

Go back to Rubidium Binding Sites List in 8z5c
Rubidium binding site 1 out of 2 in the Cystal Structure of Beta-Ketoacyl-Acp Synthase Fabf From Helicobacter Pylori


Mono view


Stereo pair view

A full contact list of Rubidium with other atoms in the Rb binding site number 1 of Cystal Structure of Beta-Ketoacyl-Acp Synthase Fabf From Helicobacter Pylori within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Rb501

b:21.4
occ:0.40
O A:ASN396 2.7 13.5 1.0
OE1 A:GLU350 2.8 11.7 1.0
OD1 A:ASN302 2.8 11.7 1.0
O A:ASN302 2.8 12.7 1.0
OG A:SER395 2.9 12.5 1.0
O A:ALA303 3.2 15.0 1.0
N A:ASN396 3.4 10.5 1.0
C A:ASN302 3.6 11.3 1.0
C A:ALA303 3.6 13.7 1.0
CB A:GLU350 3.7 15.1 1.0
C A:ASN396 3.7 13.5 1.0
CD A:GLU350 3.7 9.8 1.0
CG A:ASN302 3.8 13.4 1.0
O A:HOH652 3.9 19.5 1.0
C A:SER395 4.0 10.9 1.0
CB A:SER395 4.1 11.5 1.0
CA A:ASN396 4.1 12.2 1.0
N A:HIS304 4.1 12.3 1.0
CB A:ASN302 4.1 12.9 1.0
CA A:SER395 4.1 10.1 1.0
CG A:GLU350 4.1 11.8 1.0
O A:HOH692 4.1 14.0 1.0
CA A:HIS304 4.3 12.3 1.0
N A:ALA303 4.3 12.8 1.0
CA A:ALA303 4.5 9.9 1.0
CA A:ASN302 4.5 11.0 1.0
OG A:SER397 4.7 15.1 1.0
CB A:ASN396 4.7 13.2 1.0
NZ A:LYS336 4.7 16.2 1.0
OE2 A:GLU350 4.7 12.3 1.0
N A:SER397 4.9 9.6 1.0
O A:HOH710 4.9 16.4 1.0
O A:SER395 5.0 12.6 1.0

Rubidium binding site 2 out of 2 in 8z5c

Go back to Rubidium Binding Sites List in 8z5c
Rubidium binding site 2 out of 2 in the Cystal Structure of Beta-Ketoacyl-Acp Synthase Fabf From Helicobacter Pylori


Mono view


Stereo pair view

A full contact list of Rubidium with other atoms in the Rb binding site number 2 of Cystal Structure of Beta-Ketoacyl-Acp Synthase Fabf From Helicobacter Pylori within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Rb501

b:20.7
occ:0.38
O B:ASN396 2.7 12.7 1.0
OE1 B:GLU350 2.8 14.1 1.0
O B:ASN302 2.8 13.1 1.0
OD1 B:ASN302 2.8 13.5 1.0
OG B:SER395 2.9 14.1 1.0
O B:ALA303 3.2 14.7 1.0
N B:ASN396 3.4 13.1 1.0
C B:ASN302 3.6 15.8 1.0
C B:ALA303 3.7 14.8 1.0
CB B:GLU350 3.7 12.4 1.0
C B:ASN396 3.7 13.2 1.0
CD B:GLU350 3.7 13.7 1.0
O B:HOH637 3.8 20.4 1.0
CG B:ASN302 3.8 15.8 1.0
CB B:SER395 4.0 14.9 1.0
C B:SER395 4.0 12.6 1.0
CA B:SER395 4.1 10.8 1.0
CB B:ASN302 4.1 12.6 1.0
CA B:ASN396 4.1 16.1 1.0
N B:HIS304 4.1 12.1 1.0
CG B:GLU350 4.2 13.4 1.0
O B:HOH704 4.2 15.6 1.0
N B:ALA303 4.3 15.0 1.0
CA B:HIS304 4.3 12.5 1.0
CA B:ALA303 4.5 12.6 1.0
CA B:ASN302 4.5 11.8 1.0
OG B:SER397 4.6 16.7 1.0
NZ B:LYS336 4.7 17.1 1.0
OE2 B:GLU350 4.8 14.4 1.0
CB B:ASN396 4.8 13.7 1.0
O B:HOH670 4.9 11.8 1.0
N B:SER397 4.9 13.1 1.0
O B:SER395 5.0 12.8 1.0

Reference:

L.Zhang, Y.Huang, Y.Wang, C.Cai, L.Zhang, F.Ye. The Beta-Ketoacyl-Acp Synthase Fabf Catalyzes Carbon-Carbon Bond Formation in A Bimodal Pattern For Fatty Acid Biosynthesis. Angew.Chem.Int.Ed.Engl. 07921 2024.
ISSN: ESSN 1521-3773
PubMed: 39175097
DOI: 10.1002/ANIE.202407921
Page generated: Thu Oct 31 23:15:32 2024

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