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Sodium in PDB 1tjp: Crystal Structure of Wild-Type Tryptophan Synthase Complexed with 1- [(2-Hydroxylphenyl)Amino]3-Glycerolphosphate

Enzymatic activity of Crystal Structure of Wild-Type Tryptophan Synthase Complexed with 1- [(2-Hydroxylphenyl)Amino]3-Glycerolphosphate

All present enzymatic activity of Crystal Structure of Wild-Type Tryptophan Synthase Complexed with 1- [(2-Hydroxylphenyl)Amino]3-Glycerolphosphate:
4.2.1.20;

Protein crystallography data

The structure of Crystal Structure of Wild-Type Tryptophan Synthase Complexed with 1- [(2-Hydroxylphenyl)Amino]3-Glycerolphosphate, PDB code: 1tjp was solved by V.Kulik, E.Hartmann, M.Weyand, M.Frey, A.Gierl, D.Niks, M.F.Dunn, I.Schlichting, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.94 / 1.50
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 183.000, 59.500, 67.300, 90.00, 94.80, 90.00
R / Rfree (%) 16.7 / 19.3

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Wild-Type Tryptophan Synthase Complexed with 1- [(2-Hydroxylphenyl)Amino]3-Glycerolphosphate (pdb code 1tjp). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of Wild-Type Tryptophan Synthase Complexed with 1- [(2-Hydroxylphenyl)Amino]3-Glycerolphosphate, PDB code: 1tjp:

Sodium binding site 1 out of 1 in 1tjp

Go back to Sodium Binding Sites List in 1tjp
Sodium binding site 1 out of 1 in the Crystal Structure of Wild-Type Tryptophan Synthase Complexed with 1- [(2-Hydroxylphenyl)Amino]3-Glycerolphosphate


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Wild-Type Tryptophan Synthase Complexed with 1- [(2-Hydroxylphenyl)Amino]3-Glycerolphosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na1003

b:10.2
occ:1.00
 O B:GLY232 2.3 11.5 1.0
O B:SER308 2.3 10.5 1.0
O B:HOH1039 2.3 21.0 1.0
O B:PHE306 2.3 15.4 0.6
O B:HOH1047 2.4 12.2 1.0
O B:PHE306 2.6 15.4 0.4
C B:GLY232 3.4 9.1 1.0
C B:PHE306 3.5 14.5 0.6
C B:SER308 3.5 9.7 1.0
C B:PHE306 3.7 14.5 0.4
CG B:PRO270 3.8 9.7 1.0
CD B:PRO270 3.9 8.6 1.0
N B:SER308 3.9 12.8 1.0
CB B:PHE306 4.0 14.8 0.6
CB B:PHE306 4.0 14.8 0.4
CD2 B:PHE306 4.1 14.3 0.4
CA B:GLY232 4.1 9.0 1.0
O B:GLY268 4.1 10.4 1.0
CA B:PHE306 4.2 14.3 0.6
N B:PHE306 4.2 14.2 0.4
CA B:PHE306 4.2 14.3 0.4
O B:LEU304 4.3 13.1 0.4
OG B:SER297 4.3 14.1 0.6
CA B:SER308 4.3 11.0 1.0
CD2 B:PHE306 4.4 14.3 0.6
O B:VAL231 4.4 9.3 1.0
C B:PRO307 4.4 11.9 0.4
N B:PHE306 4.5 14.2 0.6
CG B:PHE306 4.5 14.1 0.4
N B:PRO307 4.5 12.3 0.6
N B:VAL309 4.5 9.2 1.0
N B:GLY233 4.5 8.7 1.0
CA B:VAL309 4.6 9.0 1.0
C B:PRO307 4.6 11.6 0.6
CB B:VAL309 4.6 9.4 1.0
CG B:PHE306 4.7 14.1 0.6
O B:LEU304 4.7 12.3 0.6
N B:PRO307 4.7 12.7 0.4
CA B:PRO307 4.7 12.7 0.6
CA B:PRO307 4.8 13.6 0.4
CA B:GLY233 4.8 7.7 1.0
OE2 B:GLU256 4.8 10.7 1.0
N B:GLY232 4.9 8.0 1.0

Reference:

V.Kulik, E.Hartmann, M.Weyand, M.Frey, A.Gierl, D.Niks, M.F.Dunn, I.Schlichting. On the Structural Basis of the Catalytic Mechanism and the Regulation of the Alpha Subunit of Tryptophan Synthase From Salmonella Typhimurium and BX1 From Maize, Two Evolutionarily Related Enzymes. J.Mol.Biol. V. 352 608 2005.
ISSN: ISSN 0022-2836
PubMed: 16120446
DOI: 10.1016/J.JMB.2005.07.014
Page generated: Tue Dec 15 05:36:28 2020

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