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Caesium in PDB 3cep: Structure of A Tryptophan Synthase Quinonoid Intermediate

Enzymatic activity of Structure of A Tryptophan Synthase Quinonoid Intermediate

All present enzymatic activity of Structure of A Tryptophan Synthase Quinonoid Intermediate:
4.2.1.20;

Protein crystallography data

The structure of Structure of A Tryptophan Synthase Quinonoid Intermediate, PDB code: 3cep was solved by T.R.M.Barends, T.Domratcheva, V.Kulik, L.Blumenstein, M.F.Dunn, I.Schlichting, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 23.70 / 2.10
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 184.024, 58.908, 67.086, 90.00, 95.19, 90.00
R / Rfree (%) 19.8 / 23.8

Caesium Binding Sites:

The binding sites of Caesium atom in the Structure of A Tryptophan Synthase Quinonoid Intermediate (pdb code 3cep). This binding sites where shown within 5.0 Angstroms radius around Caesium atom.
In total 3 binding sites of Caesium where determined in the Structure of A Tryptophan Synthase Quinonoid Intermediate, PDB code: 3cep:
Jump to Caesium binding site number: 1; 2; 3;

Caesium binding site 1 out of 3 in 3cep

Go back to Caesium Binding Sites List in 3cep
Caesium binding site 1 out of 3 in the Structure of A Tryptophan Synthase Quinonoid Intermediate


Mono view


Stereo pair view

A full contact list of Caesium with other atoms in the Cs binding site number 1 of Structure of A Tryptophan Synthase Quinonoid Intermediate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cs398

b:19.8
occ:1.00
O B:HOH562 2.5 11.3 1.0
O B:PHE306 3.0 11.8 1.0
O B:GLY232 3.0 15.1 1.0
O B:GLY268 3.1 15.8 1.0
O B:SER308 3.3 12.8 1.0
O B:LEU304 3.5 12.8 1.0
O B:VAL231 3.7 13.1 1.0
C B:GLY232 3.9 14.1 1.0
C B:PHE306 4.0 12.0 1.0
C B:GLY268 4.1 15.5 1.0
CD B:PRO270 4.1 13.7 1.0
CA B:GLY232 4.2 13.7 1.0
CB B:PHE306 4.3 12.5 1.0
CD B:PRO257 4.4 12.6 1.0
N B:PHE306 4.5 12.3 1.0
C B:SER308 4.5 13.0 1.0
C B:LEU304 4.5 12.3 1.0
CA B:PHE306 4.5 12.2 1.0
CG B:PRO257 4.5 13.1 1.0
C B:VAL231 4.6 13.5 1.0
CG B:PRO270 4.6 13.6 1.0
CA B:GLY268 4.6 15.2 1.0
CD2 B:PHE306 4.7 12.8 1.0
OE2 B:GLU256 4.8 11.3 1.0
N B:SER308 4.8 12.2 1.0
N B:GLY232 4.9 13.5 1.0

Caesium binding site 2 out of 3 in 3cep

Go back to Caesium Binding Sites List in 3cep
Caesium binding site 2 out of 3 in the Structure of A Tryptophan Synthase Quinonoid Intermediate


Mono view


Stereo pair view

A full contact list of Caesium with other atoms in the Cs binding site number 2 of Structure of A Tryptophan Synthase Quinonoid Intermediate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cs399

b:35.5
occ:0.50
O B:PRO56 3.1 14.8 1.0
O B:GLY54 3.3 15.9 1.0
O B:HOH566 3.5 30.2 1.0
O B:HOH456 3.5 21.6 1.0
C B:PRO56 4.2 14.6 1.0
O B:HOH549 4.3 30.2 1.0
C B:GLY54 4.4 15.6 1.0
C B:ARG55 4.8 14.9 1.0
N B:PRO56 4.8 14.8 1.0
CA B:THR57 5.0 13.9 1.0
O B:ARG55 5.0 15.1 1.0

Caesium binding site 3 out of 3 in 3cep

Go back to Caesium Binding Sites List in 3cep
Caesium binding site 3 out of 3 in the Structure of A Tryptophan Synthase Quinonoid Intermediate


Mono view


Stereo pair view

A full contact list of Caesium with other atoms in the Cs binding site number 3 of Structure of A Tryptophan Synthase Quinonoid Intermediate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cs400

b:34.7
occ:1.00
O B:THR66 3.0 19.8 1.0
O B:THR69 3.1 17.2 1.0
O B:THR71 3.1 16.4 1.0
OG1 B:THR66 3.5 20.1 1.0
C B:THR66 3.9 20.2 1.0
CB B:THR66 4.1 20.1 1.0
C B:THR69 4.1 17.5 1.0
C B:THR71 4.2 16.4 1.0
OG1 B:THR69 4.4 16.6 1.0
N B:THR71 4.5 17.0 1.0
O B:HOH435 4.6 12.9 1.0
N B:THR69 4.7 18.1 1.0
CA B:THR66 4.7 20.0 1.0
N B:ALA67 4.7 19.5 1.0
CA B:ALA67 4.8 19.5 1.0
CA B:ARG70 4.8 17.9 1.0
C B:ARG70 4.8 17.4 1.0
N B:ARG70 4.9 17.2 1.0
N B:THR72 4.9 16.1 1.0
CA B:THR69 5.0 17.3 1.0
CA B:THR71 5.0 16.2 1.0
OG1 B:THR72 5.0 15.9 1.0

Reference:

T.R.Barends, T.Domratcheva, V.Kulik, L.Blumenstein, D.Niks, M.F.Dunn, I.Schlichting. Structure and Mechanistic Implications of A Tryptophan Synthase Quinonoid Intermediate. Chembiochem V. 9 1024 2008.
ISSN: ISSN 1439-4227
PubMed: 18351684
DOI: 10.1002/CBIC.200700703
Page generated: Sun Jul 13 22:31:52 2025

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