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Chlorine in PDB 4iij: Crystal Structure of Tubulin-Stathmin-Ttl-Apo Complex

Protein crystallography data

The structure of Crystal Structure of Tubulin-Stathmin-Ttl-Apo Complex, PDB code: 4iij was solved by A.E.Prota, M.M.Magiera, M.Kuijpers, K.Bargsten, D.Frey, M.Wieser, R.Jaussi, C.C.Hoogenraad, R.A.Kammerer, C.Janke, M.O.Steinmetz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 62.28 / 2.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 103.530, 155.910, 181.020, 90.00, 90.00, 90.00
R / Rfree (%) 19.7 / 23.5

Other elements in 4iij:

The structure of Crystal Structure of Tubulin-Stathmin-Ttl-Apo Complex also contains other interesting chemical elements:

Magnesium (Mg) 5 atoms
Calcium (Ca) 3 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Tubulin-Stathmin-Ttl-Apo Complex (pdb code 4iij). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Tubulin-Stathmin-Ttl-Apo Complex, PDB code: 4iij:

Chlorine binding site 1 out of 1 in 4iij

Go back to Chlorine Binding Sites List in 4iij
Chlorine binding site 1 out of 1 in the Crystal Structure of Tubulin-Stathmin-Ttl-Apo Complex


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Tubulin-Stathmin-Ttl-Apo Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl504

b:77.7
occ:1.00
H A:LYS163 2.5 99.0 1.0
HB3 A:LYS163 2.8 0.6 1.0
HA A:TYR161 2.9 89.7 1.0
HD3 A:LYS164 3.2 0.6 1.0
H A:GLY162 3.2 83.3 1.0
HE2 A:LYS164 3.2 96.2 1.0
N A:LYS163 3.3 82.5 1.0
HD2 A:LYS164 3.4 0.6 1.0
N A:GLY162 3.4 69.4 1.0
HB2 A:LYS163 3.5 0.6 1.0
CB A:LYS163 3.6 91.3 1.0
C A:TYR161 3.6 73.2 1.0
CA A:TYR161 3.7 74.7 1.0
CD A:LYS164 3.7 83.8 1.0
CE A:LYS164 3.9 80.2 1.0
H A:LYS164 4.0 96.7 1.0
O A:HOH608 4.0 47.3 1.0
CA A:LYS163 4.0 88.7 1.0
HB3 A:TYR161 4.2 81.9 1.0
C A:GLY162 4.3 75.3 1.0
O A:TYR161 4.3 76.3 1.0
CA A:GLY162 4.3 68.7 1.0
HA3 A:GLY162 4.5 82.5 1.0
HE3 A:LYS164 4.5 96.2 1.0
CB A:TYR161 4.5 68.2 1.0
N A:LYS164 4.5 80.6 1.0
O A:ASP160 4.6 88.9 1.0
N A:TYR161 4.7 82.9 1.0
HZ3 A:LYS164 4.7 0.4 1.0
C A:LYS163 4.8 83.0 1.0
HA A:LYS163 4.8 0.4 1.0
CG A:LYS163 4.8 0.5 1.0
HG2 A:LYS163 4.8 0.8 1.0
HD2 A:TYR161 4.9 92.2 1.0
NZ A:LYS164 4.9 86.1 1.0

Reference:

A.E.Prota, M.M.Magiera, M.Kuijpers, K.Bargsten, D.Frey, M.Wieser, R.Jaussi, C.C.Hoogenraad, R.A.Kammerer, C.Janke, M.O.Steinmetz. Structural Basis of Tubulin Tyrosination By Tubulin Tyrosine Ligase. J.Cell Biol. V. 200 259 2013.
ISSN: ISSN 0021-9525
PubMed: 23358242
DOI: 10.1083/JCB.201211017
Page generated: Fri Jul 11 16:51:33 2025

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