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Aluminium in PDB 5o6e: Structure of SCPIF1 in Complex with Tttgggtt and Adp-ALF4

Enzymatic activity of Structure of SCPIF1 in Complex with Tttgggtt and Adp-ALF4

All present enzymatic activity of Structure of SCPIF1 in Complex with Tttgggtt and Adp-ALF4:
3.6.4.12;

Protein crystallography data

The structure of Structure of SCPIF1 in Complex with Tttgggtt and Adp-ALF4, PDB code: 5o6e was solved by K.Y.Lu, W.F.Chen, S.Rety, N.N.Liu, X.G.Xu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 65.21 / 3.35
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 150.605, 150.605, 136.339, 90.00, 90.00, 120.00
R / Rfree (%) 17.8 / 25.7

Other elements in 5o6e:

The structure of Structure of SCPIF1 in Complex with Tttgggtt and Adp-ALF4 also contains other interesting chemical elements:

Fluorine (F) 8 atoms
Magnesium (Mg) 2 atoms
Chlorine (Cl) 1 atom

Aluminium Binding Sites:

The binding sites of Aluminium atom in the Structure of SCPIF1 in Complex with Tttgggtt and Adp-ALF4 (pdb code 5o6e). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total 2 binding sites of Aluminium where determined in the Structure of SCPIF1 in Complex with Tttgggtt and Adp-ALF4, PDB code: 5o6e:
Jump to Aluminium binding site number: 1; 2;

Aluminium binding site 1 out of 2 in 5o6e

Go back to Aluminium Binding Sites List in 5o6e
Aluminium binding site 1 out of 2 in the Structure of SCPIF1 in Complex with Tttgggtt and Adp-ALF4


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Structure of SCPIF1 in Complex with Tttgggtt and Adp-ALF4 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Al1002

b:78.3
occ:1.00
AL A:ALF1002 0.0 78.3 1.0
F4 A:ALF1002 1.8 82.9 1.0
F1 A:ALF1002 1.8 66.1 1.0
F3 A:ALF1002 1.8 91.8 1.0
F2 A:ALF1002 1.8 79.6 1.0
O3B A:ADP1001 2.3 72.7 1.0
O2B A:ADP1001 3.1 69.4 1.0
OE2 A:GLU342 3.1 0.7 1.0
PB A:ADP1001 3.2 75.4 1.0
MG A:MG1003 3.7 74.9 1.0
NH2 A:ARG417 3.9 1.0 1.0
NZ A:LYS264 4.1 58.5 1.0
CA A:GLY709 4.2 81.4 1.0
CD A:GLU342 4.2 0.4 1.0
NH1 A:ARG734 4.2 78.3 1.0
NE2 A:GLN381 4.2 59.7 1.0
O1B A:ADP1001 4.3 77.7 1.0
N A:GLY261 4.3 81.2 1.0
OE1 A:GLN381 4.3 76.3 1.0
N A:GLY709 4.4 75.0 1.0
NH2 A:ARG734 4.4 87.4 1.0
NH1 A:ARG417 4.4 95.7 1.0
OE1 A:GLU342 4.5 0.1 1.0
O3A A:ADP1001 4.5 77.0 1.0
CE A:LYS264 4.6 58.6 1.0
CZ A:ARG417 4.6 95.2 1.0
O A:GLY709 4.7 85.4 1.0
C A:GLY709 4.7 85.1 1.0
CD A:GLN381 4.7 70.9 1.0
CA A:ALA260 4.8 98.0 1.0
CZ A:ARG734 4.8 81.5 1.0
OG A:SER265 4.9 0.8 1.0

Aluminium binding site 2 out of 2 in 5o6e

Go back to Aluminium Binding Sites List in 5o6e
Aluminium binding site 2 out of 2 in the Structure of SCPIF1 in Complex with Tttgggtt and Adp-ALF4


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 2 of Structure of SCPIF1 in Complex with Tttgggtt and Adp-ALF4 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Al1002

b:67.6
occ:1.00
AL B:ALF1002 0.0 67.6 1.0
F4 B:ALF1002 1.8 67.3 1.0
F1 B:ALF1002 1.8 58.0 1.0
F3 B:ALF1002 1.8 80.0 1.0
F2 B:ALF1002 1.8 66.8 1.0
O2B B:ADP1001 2.3 69.4 1.0
OE2 B:GLU342 3.2 0.6 1.0
O1B B:ADP1001 3.3 72.8 1.0
PB B:ADP1001 3.3 73.7 1.0
MG B:MG1003 3.4 68.3 1.0
NH2 B:ARG734 3.7 82.7 1.0
NH1 B:ARG734 3.9 82.5 1.0
NE2 B:GLN381 4.0 66.0 1.0
OE1 B:GLN381 4.2 76.7 1.0
NH2 B:ARG417 4.2 67.0 1.0
CA B:GLY709 4.2 84.4 1.0
CD B:GLU342 4.2 97.4 1.0
CZ B:ARG734 4.3 81.9 1.0
N B:GLY261 4.3 68.7 1.0
N B:GLY709 4.3 81.9 1.0
NH1 B:ARG417 4.3 65.7 1.0
O3A B:ADP1001 4.4 76.8 1.0
CA B:ALA260 4.4 77.1 1.0
OE1 B:GLU342 4.4 0.9 1.0
NZ B:LYS264 4.5 55.8 1.0
O3B B:ADP1001 4.5 73.5 1.0
CD B:GLN381 4.6 71.5 1.0
CE B:LYS264 4.7 59.9 1.0
CZ B:ARG417 4.8 66.8 1.0
C B:GLY709 4.8 87.9 1.0
CB B:ALA260 4.8 76.0 1.0
O B:GLY709 4.8 88.8 1.0
C B:ALA260 4.9 71.5 1.0

Reference:

K.Y.Lu, W.F.Chen, S.Rety, N.N.Liu, W.Q.Wu, Y.X.Dai, D.Li, H.Y.Ma, S.X.Dou, X.G.Xi. Insights Into the Structural and Mechanistic Basis of Multifunctional S. Cerevisiae PIF1P Helicase. Nucleic Acids Res. V. 46 1486 2018.
ISSN: ESSN 1362-4962
PubMed: 29202194
DOI: 10.1093/NAR/GKX1217
Page generated: Sat Dec 12 01:34:00 2020

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