Phosphorus in PDB 1a5s: Crystal Structure of Wild-Type Tryptophan Synthase Complexed with 5- Fluoroindole Propanol Phosphate and L-Ser Bound As Amino Acrylate to the Beta Site

Enzymatic activity of Crystal Structure of Wild-Type Tryptophan Synthase Complexed with 5- Fluoroindole Propanol Phosphate and L-Ser Bound As Amino Acrylate to the Beta Site

All present enzymatic activity of Crystal Structure of Wild-Type Tryptophan Synthase Complexed with 5- Fluoroindole Propanol Phosphate and L-Ser Bound As Amino Acrylate to the Beta Site:
4.2.1.20;

Protein crystallography data

The structure of Crystal Structure of Wild-Type Tryptophan Synthase Complexed with 5- Fluoroindole Propanol Phosphate and L-Ser Bound As Amino Acrylate to the Beta Site, PDB code: 1a5s 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, 60.800, 67.500, 90.00, 94.60, 90.00
R / Rfree (%) 17.7 / 24.7

Phosphorus Binding Sites:

The binding sites of Phosphorus atom in the Crystal Structure of Wild-Type Tryptophan Synthase Complexed with 5- Fluoroindole Propanol Phosphate and L-Ser Bound As Amino Acrylate to the Beta Site (pdb code 1a5s). This binding sites where shown within 5.0 Angstroms radius around Phosphorus atom.
In total 2 binding sites of Phosphorus where determined in the Crystal Structure of Wild-Type Tryptophan Synthase Complexed with 5- Fluoroindole Propanol Phosphate and L-Ser Bound As Amino Acrylate to the Beta Site, PDB code: 1a5s:
Jump to Phosphorus binding site number: 1; 2;

Phosphorus binding site 1 out of 2 in 1a5s

Go back to Phosphorus Binding Sites List in 1a5s
Phosphorus binding site 1 out of 2 in the Crystal Structure of Wild-Type Tryptophan Synthase Complexed with 5- Fluoroindole Propanol Phosphate and L-Ser Bound As Amino Acrylate to the Beta Site


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 1 of Crystal Structure of Wild-Type Tryptophan Synthase Complexed with 5- Fluoroindole Propanol Phosphate and L-Ser Bound As Amino Acrylate to the Beta Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:P270

b:37.8
occ:1.00
 P A:FIP270 0.0 37.8 1.0
OP1 A:FIP270 1.5 27.6 1.0
OP2 A:FIP270 1.5 34.8 1.0
OP3 A:FIP270 1.5 32.9 1.0
OP4 A:FIP270 1.6 39.2 1.0
C1P A:FIP270 2.7 36.9 1.0
N A:SER235 3.6 33.5 1.0
O A:HOH1050 3.6 33.8 1.0
OG A:SER235 3.8 30.2 1.0
O A:HOH1129 3.8 34.0 1.0
N A:GLY213 3.8 34.6 1.0
N A:GLY234 3.9 32.7 1.0
C2P A:FIP270 4.0 33.1 1.0
CA A:PHE212 4.0 39.1 1.0
CB A:SER235 4.0 37.2 1.0
N A:GLY184 4.1 45.7 1.0
CB A:THR183 4.2 35.4 1.0
CA A:GLY234 4.3 30.9 1.0
N A:PHE212 4.4 36.1 1.0
CA A:THR183 4.4 39.3 1.0
C A:PHE212 4.4 36.4 1.0
CD1 A:PHE212 4.5 48.7 1.0
CA A:SER235 4.5 35.1 1.0
C A:GLY234 4.5 31.8 1.0
C A:THR183 4.6 43.9 1.0
C A:GLY184 4.7 51.5 1.0
N A:ALA185 4.7 53.6 1.0
CG2 A:THR183 4.8 30.3 1.0
CA A:GLY184 4.8 48.8 1.0
CA A:GLY213 4.9 37.3 1.0
O A:GLY184 4.9 50.5 1.0

Phosphorus binding site 2 out of 2 in 1a5s

Go back to Phosphorus Binding Sites List in 1a5s
Phosphorus binding site 2 out of 2 in the Crystal Structure of Wild-Type Tryptophan Synthase Complexed with 5- Fluoroindole Propanol Phosphate and L-Ser Bound As Amino Acrylate to the Beta Site


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 2 of Crystal Structure of Wild-Type Tryptophan Synthase Complexed with 5- Fluoroindole Propanol Phosphate and L-Ser Bound As Amino Acrylate to the Beta Site within 5.0Å range:
probe atom residue distance (Å) B Occ
B:P901

b:8.4
occ:1.00
 P B:PLP901 0.0 8.4 1.0
O2P B:PLP901 1.5 14.6 1.0
O3P B:PLP901 1.5 12.8 1.0
O1P B:PLP901 1.5 10.4 1.0
O4P B:PLP901 1.6 7.2 1.0
C5A B:PLP901 2.6 17.4 1.0
OG B:SER235 3.3 9.1 1.0
N B:SER235 3.5 5.2 1.0
C5 B:PLP901 3.6 23.0 1.0
N B:GLY234 3.6 7.7 1.0
O B:HOH1087 3.7 22.5 1.0
N B:ASN236 3.7 8.7 1.0
O B:HOH1053 3.8 10.5 1.0
ND2 B:ASN236 3.8 4.3 1.0
N B:GLY233 3.9 13.9 1.0
NZ B:LYS87 4.1 34.9 1.0
OG1 B:THR190 4.1 13.8 1.0
C6 B:PLP901 4.1 26.9 1.0
NE2 B:HIS86 4.2 5.9 1.0
C B:GLY234 4.2 5.9 1.0
N B:GLY232 4.2 10.1 1.0
CA B:SER235 4.2 7.1 1.0
CB B:SER235 4.2 5.8 1.0
CA B:GLY234 4.2 5.1 1.0
C4 B:PLP901 4.4 28.1 1.0
C B:SER235 4.5 5.3 1.0
CE1 B:HIS86 4.5 3.1 1.0
CB B:ASN236 4.5 8.5 1.0
C B:GLY233 4.5 10.7 1.0
CA B:GLY233 4.6 9.7 1.0
CA B:GLY232 4.6 10.1 1.0
C4A B:PLP901 4.6 27.2 1.0
CG B:ASN236 4.7 6.8 1.0
CA B:ASN236 4.7 13.3 1.0
C B:GLY232 4.8 15.2 1.0
CB B:THR190 4.9 12.6 1.0
CE B:LYS87 5.0 26.8 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: Fri Sep 25 12:16:44 2020

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