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Iodine in PDB 4tqd: Crystal Structure of the C-Terminal Domain of Ifrs Bound with 3-Iodo- L-Phe and Atp

Enzymatic activity of Crystal Structure of the C-Terminal Domain of Ifrs Bound with 3-Iodo- L-Phe and Atp

All present enzymatic activity of Crystal Structure of the C-Terminal Domain of Ifrs Bound with 3-Iodo- L-Phe and Atp:
6.1.1.26;

Protein crystallography data

The structure of Crystal Structure of the C-Terminal Domain of Ifrs Bound with 3-Iodo- L-Phe and Atp, PDB code: 4tqd was solved by A.Nakamura, P.O'donoghue, D.Soll, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.06 / 2.14
Space group P 64
Cell size a, b, c (Å), α, β, γ (°) 104.700, 104.700, 70.660, 90.00, 90.00, 120.00
R / Rfree (%) 15.5 / 19.3

Other elements in 4tqd:

The structure of Crystal Structure of the C-Terminal Domain of Ifrs Bound with 3-Iodo- L-Phe and Atp also contains other interesting chemical elements:

Magnesium (Mg) 3 atoms

Iodine Binding Sites:

The binding sites of Iodine atom in the Crystal Structure of the C-Terminal Domain of Ifrs Bound with 3-Iodo- L-Phe and Atp (pdb code 4tqd). This binding sites where shown within 5.0 Angstroms radius around Iodine atom.
In total 2 binding sites of Iodine where determined in the Crystal Structure of the C-Terminal Domain of Ifrs Bound with 3-Iodo- L-Phe and Atp, PDB code: 4tqd:
Jump to Iodine binding site number: 1; 2;

Iodine binding site 1 out of 2 in 4tqd

Go back to Iodine Binding Sites List in 4tqd
Iodine binding site 1 out of 2 in the Crystal Structure of the C-Terminal Domain of Ifrs Bound with 3-Iodo- L-Phe and Atp


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 1 of Crystal Structure of the C-Terminal Domain of Ifrs Bound with 3-Iodo- L-Phe and Atp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:I505

b:0.9
occ:0.53
I1 A:33S505 0.0 0.9 0.5
CD1 A:33S505 1.8 79.8 0.5
CE1 A:33S505 2.1 70.9 0.5
CG A:33S505 2.5 81.8 0.5
CB A:33S505 2.7 65.8 0.5
CE1 A:33S505 3.0 65.3 0.5
CZ A:33S505 3.0 46.6 0.5
O A:33S505 3.0 80.2 0.5
CD1 A:33S505 3.0 70.2 0.5
C A:33S505 3.6 38.4 0.5
CG1 A:ILE348 3.6 55.7 1.0
CA A:33S505 3.7 64.4 0.5
CD1 A:ILE348 3.7 47.9 1.0
CB A:SER346 3.8 38.0 1.0
I1 A:33S505 3.8 98.3 0.5
CD2 A:33S505 3.9 69.9 0.5
CZ A:33S505 4.1 63.6 0.5
OG A:SER346 4.2 44.8 1.0
CD1 A:LEU305 4.3 31.8 1.0
CE2 A:33S505 4.3 49.8 0.5
CG A:33S505 4.4 71.8 0.5
CA A:ALA302 4.4 37.6 1.0
CE2 A:33S505 4.5 61.9 0.5
O A:PHE347 4.5 33.7 1.0
OXT A:33S505 4.5 44.1 0.5
CB A:ALA302 4.6 31.2 1.0
O A:ALA420 4.6 36.4 1.0
N A:ALA302 4.8 39.4 1.0
CD2 A:33S505 4.8 59.5 0.5
CA A:SER346 4.9 31.3 1.0
N A:ALA420 4.9 33.8 1.0
N A:33S505 4.9 57.8 0.5
O A:33S505 4.9 46.5 0.5

Iodine binding site 2 out of 2 in 4tqd

Go back to Iodine Binding Sites List in 4tqd
Iodine binding site 2 out of 2 in the Crystal Structure of the C-Terminal Domain of Ifrs Bound with 3-Iodo- L-Phe and Atp


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 2 of Crystal Structure of the C-Terminal Domain of Ifrs Bound with 3-Iodo- L-Phe and Atp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:I505

b:98.3
occ:0.47
I1 A:33S505 0.0 98.3 0.5
CE1 A:33S505 2.1 65.3 0.5
CZ A:33S505 3.1 63.6 0.5
CD1 A:33S505 3.1 79.8 0.5
CE2 A:TYR306 3.8 48.8 1.0
I1 A:33S505 3.8 0.9 0.5
CZ A:TYR306 3.8 49.0 1.0
CD2 A:TYR306 4.0 44.8 1.0
CB A:ALA302 4.0 31.2 1.0
CE1 A:TYR306 4.1 41.8 1.0
CH2 A:TRP417 4.1 46.1 1.0
CD1 A:ILE348 4.2 47.9 1.0
CG A:TYR306 4.2 40.7 1.0
O A:ALA302 4.3 37.0 1.0
CD1 A:TYR306 4.3 36.4 1.0
CA A:ALA302 4.3 37.6 1.0
CZ3 A:TRP417 4.3 38.4 1.0
OH A:TYR306 4.4 49.6 1.0
CZ A:33S505 4.4 46.6 0.5
CE2 A:33S505 4.4 61.9 0.5
CG A:33S505 4.5 81.8 0.5
CZ2 A:TRP417 4.5 42.0 1.0
CE1 A:33S505 4.5 70.9 0.5
C A:ALA302 4.7 34.2 1.0
O A:33S505 4.9 80.2 0.5
CG1 A:ILE348 4.9 55.7 1.0
CE3 A:TRP417 4.9 37.5 1.0
CD2 A:33S505 5.0 69.9 0.5
CE2 A:TRP417 5.0 37.2 1.0

Reference:

L.T.Guo, Y.S.Wang, A.Nakamura, D.Eiler, J.Kavran, M.Wong, L.Kiessling, T.Steitz, P.O'donoghue, D.Soll. Polyspecific Pyrrolysyl-Trna Synthetases From Directed Evolution Proc.Natl.Acad.Sci.Usa 2014.
ISSN: ESSN 1091-6490
Page generated: Fri Aug 8 18:47:22 2025

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