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

Last articles

Zn in 8PFC
Zn in 8SF0
Zn in 8SOJ
Zn in 8SOK
Zn in 8SYI
Zn in 8SLG
Zn in 8SEX
Zn in 8SEZ
Zn in 8SJG
Zn in 8SEY
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy