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Fluorine in PDB 1a50: Crystal Structure of Wild-Type Tryptophan Synthase Complexed with 5- Fluoroindole Propanol Phosphate

Enzymatic activity of Crystal Structure of Wild-Type Tryptophan Synthase Complexed with 5- Fluoroindole Propanol Phosphate

All present enzymatic activity of Crystal Structure of Wild-Type Tryptophan Synthase Complexed with 5- Fluoroindole Propanol Phosphate:
4.2.1.20;

Protein crystallography data

The structure of Crystal Structure of Wild-Type Tryptophan Synthase Complexed with 5- Fluoroindole Propanol Phosphate, PDB code: 1a50 was solved by T.R.Schneider, E.Gerhardt, M.Lee, P.-H.Liang, K.S.Anderson, I.Schlichting, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.30
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 182.700, 60.700, 67.500, 90.00, 94.50, 90.00
R / Rfree (%) 17.7 / 24.7

Other elements in 1a50:

The structure of Crystal Structure of Wild-Type Tryptophan Synthase Complexed with 5- Fluoroindole Propanol Phosphate also contains other interesting chemical elements:

Sodium (Na) 1 atom

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of Wild-Type Tryptophan Synthase Complexed with 5- Fluoroindole Propanol Phosphate (pdb code 1a50). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Crystal Structure of Wild-Type Tryptophan Synthase Complexed with 5- Fluoroindole Propanol Phosphate, PDB code: 1a50:

Fluorine binding site 1 out of 1 in 1a50

Go back to Fluorine Binding Sites List in 1a50
Fluorine binding site 1 out of 1 in the Crystal Structure of Wild-Type Tryptophan Synthase Complexed with 5- Fluoroindole Propanol Phosphate


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of Wild-Type Tryptophan Synthase Complexed with 5- Fluoroindole Propanol Phosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F270

b:21.5
occ:1.00
F A:FIP270 0.0 21.5 1.0
C5 A:FIP270 1.3 18.7 1.0
C4 A:FIP270 2.4 14.2 1.0
C6 A:FIP270 2.4 18.6 1.0
CD1 A:ILE153 2.9 20.8 1.0
C9 A:FIP270 3.6 15.9 1.0
C7 A:FIP270 3.6 16.1 1.0
CE1 A:TYR175 3.9 15.4 1.0
CE1 A:PHE212 4.0 41.0 1.0
C8 A:FIP270 4.1 12.2 1.0
CZ A:PHE212 4.1 42.6 1.0
CG1 A:ILE153 4.2 20.7 1.0
CZ A:TYR175 4.2 18.2 1.0
O B:HOH1183 4.3 37.2 1.0
OH A:TYR175 4.3 21.1 1.0
CD1 A:TYR175 4.4 16.5 1.0
CD1 A:LEU127 4.7 14.3 1.0
CD2 A:LEU100 4.9 16.4 1.0
CE2 A:TYR175 4.9 20.7 1.0
C3 A:FIP270 4.9 15.2 1.0
CD1 A:PHE212 5.0 39.7 1.0

Reference:

T.R.Schneider, E.Gerhardt, M.Lee, P.H.Liang, K.S.Anderson, I.Schlichting. Loop Closure and Intersubunit Communication in Tryptophan Synthase. Biochemistry V. 37 5394 1998.
ISSN: ISSN 0006-2960
PubMed: 9548921
DOI: 10.1021/BI9728957
Page generated: Sun Dec 13 11:28:05 2020

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