Phosphorus 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

Phosphorus Binding Sites:

The binding sites of Phosphorus 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 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, PDB code: 1a50:
Jump to Phosphorus binding site number: 1; 2;

Phosphorus binding site 1 out of 2 in 1a50

Go back to Phosphorus Binding Sites List in 1a50
Phosphorus binding site 1 out of 2 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 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 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:P270

b:22.6
occ:1.00
P A:FIP270 0.0 22.6 1.0
OP3 A:FIP270 1.5 15.6 1.0
OP1 A:FIP270 1.5 20.0 1.0
OP2 A:FIP270 1.5 21.9 1.0
OP4 A:FIP270 1.6 20.4 1.0
C1P A:FIP270 2.6 22.9 1.0
O A:HOH1158 3.5 21.6 1.0
N A:SER235 3.6 14.7 1.0
OG A:SER235 3.7 15.8 1.0
N A:GLY213 3.8 24.3 1.0
N A:GLY234 3.9 17.6 1.0
O A:HOH1113 3.9 16.0 1.0
C2P A:FIP270 3.9 21.4 1.0
N A:GLY184 4.0 35.2 1.0
CA A:PHE212 4.0 26.8 1.0
CB A:THR183 4.1 30.4 1.0
CB A:SER235 4.2 15.8 1.0
CA A:GLY234 4.2 14.9 1.0
CA A:THR183 4.4 33.1 1.0
N A:PHE212 4.4 20.5 1.0
C A:PHE212 4.4 26.4 1.0
C A:GLY234 4.4 16.4 1.0
CA A:SER235 4.5 17.2 1.0
C A:THR183 4.6 35.7 1.0
CD1 A:PHE212 4.6 39.7 1.0
C A:GLY184 4.6 42.7 1.0
CG2 A:THR183 4.7 28.3 1.0
CA A:GLY184 4.8 39.5 1.0
CA A:GLY213 4.8 24.8 1.0
O A:GLY184 4.8 41.5 1.0
N A:ALA185 4.9 43.9 1.0
C A:SER233 5.0 15.6 1.0

Phosphorus binding site 2 out of 2 in 1a50

Go back to Phosphorus Binding Sites List in 1a50
Phosphorus binding site 2 out of 2 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 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 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:P901

b:9.3
occ:1.00
P B:PLP901 0.0 9.3 1.0
O2P B:PLP901 1.5 12.3 1.0
O3P B:PLP901 1.5 10.9 1.0
O1P B:PLP901 1.5 13.6 1.0
O4P B:PLP901 1.5 8.2 1.0
C5A B:PLP901 2.6 13.2 1.0
OG B:SER235 3.4 6.5 1.0
N B:SER235 3.5 2.7 1.0
O B:HOH1022 3.5 4.2 1.0
O B:HOH1040 3.6 17.5 1.0
N B:GLY234 3.6 3.9 1.0
C5 B:PLP901 3.6 14.8 1.0
N B:GLY233 3.8 6.9 1.0
N B:ASN236 3.9 3.1 1.0
OD1 B:ASN236 4.1 4.8 1.0
OG1 B:THR190 4.1 8.9 1.0
N B:GLY232 4.2 5.3 1.0
NE2 B:HIS86 4.2 4.1 1.0
C B:GLY234 4.2 2.0 1.0
CA B:SER235 4.2 2.4 1.0
C6 B:PLP901 4.3 12.5 1.0
CA B:GLY234 4.3 2.0 1.0
CB B:SER235 4.3 2.9 1.0
CE1 B:HIS86 4.4 2.0 1.0
C4 B:PLP901 4.4 15.7 1.0
C4A B:PLP901 4.5 12.5 1.0
C B:GLY233 4.5 6.1 1.0
CA B:GLY233 4.5 3.7 1.0
C B:SER235 4.6 2.0 1.0
CA B:GLY232 4.6 4.8 1.0
C B:GLY232 4.7 8.2 1.0
CB B:ASN236 4.8 6.7 1.0
CG B:ASN236 4.8 7.4 1.0
CA B:ASN236 4.9 7.3 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 12:14:13 2020

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