Atomistry » Sodium » PDB 7rnp-7s31 » 7rof
Atomistry »
  Sodium »
    PDB 7rnp-7s31 »
      7rof »

Sodium in PDB 7rof: Engineered Tryptophan Synthase B-Subunit From Pyrococcus Furiosus, PFTRPB2B9-H275E with L-Trp Non-Covalently Bound

Enzymatic activity of Engineered Tryptophan Synthase B-Subunit From Pyrococcus Furiosus, PFTRPB2B9-H275E with L-Trp Non-Covalently Bound

All present enzymatic activity of Engineered Tryptophan Synthase B-Subunit From Pyrococcus Furiosus, PFTRPB2B9-H275E with L-Trp Non-Covalently Bound:
4.2.1.20;

Protein crystallography data

The structure of Engineered Tryptophan Synthase B-Subunit From Pyrococcus Furiosus, PFTRPB2B9-H275E with L-Trp Non-Covalently Bound, PDB code: 7rof was solved by P.M.Higgins, A.R.Buller, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.70 / 2.39
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 57.402, 82.658, 322.255, 90, 90, 90
R / Rfree (%) 22.7 / 27.1

Sodium Binding Sites:

The binding sites of Sodium atom in the Engineered Tryptophan Synthase B-Subunit From Pyrococcus Furiosus, PFTRPB2B9-H275E with L-Trp Non-Covalently Bound (pdb code 7rof). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 4 binding sites of Sodium where determined in the Engineered Tryptophan Synthase B-Subunit From Pyrococcus Furiosus, PFTRPB2B9-H275E with L-Trp Non-Covalently Bound, PDB code: 7rof:
Jump to Sodium binding site number: 1; 2; 3; 4;

Sodium binding site 1 out of 4 in 7rof

Go back to Sodium Binding Sites List in 7rof
Sodium binding site 1 out of 4 in the Engineered Tryptophan Synthase B-Subunit From Pyrococcus Furiosus, PFTRPB2B9-H275E with L-Trp Non-Covalently Bound


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Engineered Tryptophan Synthase B-Subunit From Pyrococcus Furiosus, PFTRPB2B9-H275E with L-Trp Non-Covalently Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na402

b:51.2
occ:1.00
O A:GLY303 2.6 52.2 1.0
O A:SER263 2.8 51.0 1.0
O A:TYR301 2.9 56.3 1.0
O A:GLY227 3.0 50.3 1.0
OG A:SER265 3.4 59.4 1.0
OE2 A:GLU251 3.7 60.1 1.0
C A:GLY303 3.8 53.0 1.0
C A:SER263 4.0 51.2 1.0
C A:TYR301 4.0 58.0 1.0
C A:GLY227 4.0 50.4 1.0
CB A:SER263 4.1 50.7 1.0
CB A:SER265 4.3 58.5 1.0
O A:LEU299 4.3 52.6 1.0
CA A:GLY227 4.4 50.1 1.0
O A:VAL226 4.4 53.3 1.0
N A:GLY303 4.5 56.4 1.0
N A:SER265 4.5 55.5 1.0
CB A:VAL304 4.5 48.9 1.0
CB A:TYR301 4.6 62.3 1.0
CA A:SER263 4.6 51.5 1.0
CD2 A:TYR301 4.6 68.2 1.0
CD A:GLU251 4.6 59.6 1.0
C A:PRO302 4.6 58.1 1.0
N A:VAL304 4.7 52.2 1.0
CA A:TYR301 4.7 60.0 1.0
CA A:GLY303 4.8 55.8 1.0
CA A:VAL304 4.8 50.2 1.0
CG A:GLU251 4.9 56.2 1.0
N A:TYR301 4.9 57.9 1.0
O A:PRO302 5.0 58.5 1.0
N A:PRO302 5.0 59.0 1.0

Sodium binding site 2 out of 4 in 7rof

Go back to Sodium Binding Sites List in 7rof
Sodium binding site 2 out of 4 in the Engineered Tryptophan Synthase B-Subunit From Pyrococcus Furiosus, PFTRPB2B9-H275E with L-Trp Non-Covalently Bound


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Engineered Tryptophan Synthase B-Subunit From Pyrococcus Furiosus, PFTRPB2B9-H275E with L-Trp Non-Covalently Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na401

b:85.6
occ:1.00
O B:SER263 2.6 103.5 1.0
O B:TYR301 2.7 88.0 1.0
O B:GLY303 2.9 102.0 1.0
OG B:SER265 3.2 102.7 1.0
O B:GLY227 3.2 79.9 1.0
C B:SER263 3.8 105.1 1.0
C B:TYR301 3.9 88.3 1.0
C B:GLY303 4.0 101.2 1.0
CB B:SER263 4.1 107.3 1.0
CB B:SER265 4.2 101.7 1.0
O B:LEU299 4.2 86.8 1.0
C B:GLY227 4.2 77.2 1.0
N B:SER265 4.3 103.4 1.0
CA B:SER263 4.4 106.4 1.0
C B:PRO302 4.5 107.9 1.0
O B:PRO302 4.5 108.5 1.0
CB B:TYR301 4.6 91.0 1.0
CA B:TYR301 4.6 89.9 1.0
N B:GLY303 4.6 105.1 1.0
CA B:GLY227 4.6 76.8 1.0
O B:VAL226 4.7 79.3 1.0
N B:TYR301 4.7 89.9 1.0
CB B:VAL304 4.7 97.9 1.0
N B:VAL304 4.7 99.2 1.0
OE2 B:GLU251 4.8 96.8 1.0
N B:ALA264 4.8 105.9 1.0
CA B:VAL304 4.8 97.0 1.0
N B:PRO302 4.9 110.5 1.0
CA B:SER265 4.9 102.6 1.0
CA B:GLY303 4.9 103.0 1.0
CA B:PRO302 5.0 110.6 1.0
CD2 B:TYR301 5.0 94.8 1.0

Sodium binding site 3 out of 4 in 7rof

Go back to Sodium Binding Sites List in 7rof
Sodium binding site 3 out of 4 in the Engineered Tryptophan Synthase B-Subunit From Pyrococcus Furiosus, PFTRPB2B9-H275E with L-Trp Non-Covalently Bound


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 3 of Engineered Tryptophan Synthase B-Subunit From Pyrococcus Furiosus, PFTRPB2B9-H275E with L-Trp Non-Covalently Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Na401

b:85.2
occ:1.00
O C:GLY303 2.7 81.1 1.0
O C:SER263 2.7 99.4 1.0
O C:TYR301 2.8 104.9 1.0
O C:GLY227 2.9 80.8 1.0
OG C:SER265 3.2 101.5 1.0
OE2 C:GLU251 3.8 82.7 1.0
C C:GLY303 3.9 82.3 1.0
C C:GLY227 3.9 79.3 1.0
C C:SER263 3.9 101.1 1.0
C C:TYR301 4.0 106.2 1.0
CA C:GLY227 4.2 78.2 1.0
CB C:SER263 4.2 101.5 1.0
CB C:SER265 4.2 101.8 1.0
O C:LEU299 4.3 97.6 1.0
N C:SER265 4.4 102.1 1.0
CB C:VAL304 4.6 77.6 1.0
CA C:SER263 4.6 102.4 1.0
O C:VAL226 4.6 78.1 1.0
N C:VAL304 4.7 80.9 1.0
CD C:GLU251 4.7 81.6 1.0
CA C:VAL304 4.7 78.1 1.0
C C:PRO302 4.7 87.2 1.0
CB C:TYR301 4.7 105.6 1.0
CD2 C:TYR301 4.7 106.0 1.0
N C:GLY303 4.7 86.2 1.0
CA C:TYR301 4.8 106.1 1.0
O C:PRO302 4.8 87.6 1.0
N C:TYR301 4.9 105.1 1.0
CG2 C:VAL304 4.9 75.6 1.0
CA C:GLY303 4.9 85.2 1.0
N C:ALA264 5.0 102.0 1.0
CA C:SER265 5.0 102.7 1.0
CG C:GLU251 5.0 78.8 1.0

Sodium binding site 4 out of 4 in 7rof

Go back to Sodium Binding Sites List in 7rof
Sodium binding site 4 out of 4 in the Engineered Tryptophan Synthase B-Subunit From Pyrococcus Furiosus, PFTRPB2B9-H275E with L-Trp Non-Covalently Bound


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 4 of Engineered Tryptophan Synthase B-Subunit From Pyrococcus Furiosus, PFTRPB2B9-H275E with L-Trp Non-Covalently Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Na402

b:87.6
occ:1.00
O D:GLY303 2.6 79.7 1.0
O D:SER263 2.7 107.3 1.0
O D:TYR301 2.8 87.9 1.0
OG D:SER265 3.1 102.0 1.0
O D:GLY227 3.1 78.2 1.0
C D:GLY303 3.8 79.6 1.0
C D:SER263 3.9 108.8 1.0
C D:TYR301 3.9 91.0 1.0
CB D:SER263 4.0 108.9 1.0
CB D:SER265 4.1 102.1 1.0
C D:GLY227 4.1 75.1 1.0
O D:PRO302 4.2 89.5 1.0
C D:PRO302 4.3 89.9 1.0
N D:SER265 4.3 106.9 1.0
O D:LEU299 4.4 84.6 1.0
N D:GLY303 4.4 87.3 1.0
CA D:SER263 4.5 109.0 1.0
CA D:GLY227 4.5 74.6 1.0
N D:VAL304 4.6 76.4 1.0
OE2 D:GLU251 4.6 87.8 1.0
O D:VAL226 4.6 75.8 1.0
CB D:VAL304 4.7 71.7 1.0
CA D:GLY303 4.7 83.6 1.0
CA D:TYR301 4.7 91.8 1.0
CA D:VAL304 4.7 72.6 1.0
CB D:TYR301 4.8 89.3 1.0
N D:TYR301 4.8 91.6 1.0
CA D:SER265 4.8 104.5 1.0
N D:PRO302 4.9 93.1 1.0
CA D:PRO302 4.9 93.3 1.0
CD2 D:TYR301 5.0 86.0 1.0
N D:ALA264 5.0 110.8 1.0

Reference:

P.M.Higgins, A.R.Buller. Direct Assessment of Promiscuity During Protein Engineering By Substrate Multiplexed Screening To Be Published.
Page generated: Wed Oct 9 08:39:21 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy