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Aluminium in PDB 6hpu: Crystal Structure of Human PIF1 Helicase in Complex with Adp-ALF4

Enzymatic activity of Crystal Structure of Human PIF1 Helicase in Complex with Adp-ALF4

All present enzymatic activity of Crystal Structure of Human PIF1 Helicase in Complex with Adp-ALF4:
3.6.4.12;

Protein crystallography data

The structure of Crystal Structure of Human PIF1 Helicase in Complex with Adp-ALF4, PDB code: 6hpu was solved by V.M.Levdikov, S.Dehghani-Tafti, B.D.Bax, C.M.Sanders, A.A.Antson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 91.03 / 3.96
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 209.850, 209.850, 78.885, 90.00, 90.00, 120.00
R / Rfree (%) 17.5 / 25.3

Other elements in 6hpu:

The structure of Crystal Structure of Human PIF1 Helicase in Complex with Adp-ALF4 also contains other interesting chemical elements:

Fluorine (F) 8 atoms
Magnesium (Mg) 2 atoms

Aluminium Binding Sites:

The binding sites of Aluminium atom in the Crystal Structure of Human PIF1 Helicase in Complex with Adp-ALF4 (pdb code 6hpu). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total 2 binding sites of Aluminium where determined in the Crystal Structure of Human PIF1 Helicase in Complex with Adp-ALF4, PDB code: 6hpu:
Jump to Aluminium binding site number: 1; 2;

Aluminium binding site 1 out of 2 in 6hpu

Go back to Aluminium Binding Sites List in 6hpu
Aluminium binding site 1 out of 2 in the Crystal Structure of Human PIF1 Helicase in Complex with Adp-ALF4


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Crystal Structure of Human PIF1 Helicase in Complex with Adp-ALF4 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Al802

b:0.6
occ:1.00
AL A:ALF802 0.0 0.6 1.0
F1 A:ALF802 1.8 0.4 1.0
F2 A:ALF802 1.8 0.2 1.0
F4 A:ALF802 1.8 0.6 1.0
F3 A:ALF802 1.8 0.9 1.0
O1B A:ADP801 2.2 0.5 1.0
PB A:ADP801 3.2 0.1 1.0
O3B A:ADP801 3.4 0.5 1.0
OE2 A:GLU307 3.4 0.3 1.0
OE1 A:GLN346 3.5 0.1 1.0
NH2 A:ARG584 3.6 0.9 1.0
MG A:MG803 3.6 0.8 1.0
O2B A:ADP801 3.7 0.1 1.0
NZ A:LYS234 3.7 0.4 1.0
NE2 A:GLN346 3.8 0.2 1.0
NH1 A:ARG584 3.8 0.9 1.0
NH1 A:ARG381 4.0 0.3 1.0
CD A:GLN346 4.1 0.1 1.0
N A:GLY559 4.1 0.9 1.0
CA A:GLY559 4.2 0.1 1.0
NH2 A:ARG381 4.2 0.8 1.0
CZ A:ARG584 4.2 0.2 1.0
CD A:GLU307 4.4 0.5 1.0
C A:GLY559 4.4 0.6 1.0
CZ A:ARG381 4.6 0.6 1.0
N A:GLY231 4.6 0.6 1.0
O3A A:ADP801 4.6 0.6 1.0
CA A:ALA230 4.6 0.1 1.0
CE A:LYS234 4.6 0.8 1.0
O A:GLY559 4.7 0.1 1.0
OE1 A:GLU307 4.7 0.7 1.0
N A:MET560 4.9 0.4 1.0
O A:MET560 4.9 0.4 1.0
CB A:ALA230 4.9 0.4 1.0
O1A A:ADP801 5.0 0.2 1.0

Aluminium binding site 2 out of 2 in 6hpu

Go back to Aluminium Binding Sites List in 6hpu
Aluminium binding site 2 out of 2 in the Crystal Structure of Human PIF1 Helicase in Complex with Adp-ALF4


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 2 of Crystal Structure of Human PIF1 Helicase in Complex with Adp-ALF4 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Al802

b:99.8
occ:1.00
AL B:ALF802 0.0 99.8 1.0
F1 B:ALF802 1.8 79.1 1.0
F2 B:ALF802 1.8 0.2 1.0
F3 B:ALF802 1.8 0.6 1.0
F4 B:ALF802 1.8 81.0 1.0
O3B B:ADP801 2.3 0.6 1.0
PB B:ADP801 3.2 0.6 1.0
OE2 B:GLU307 3.4 0.6 1.0
O2B B:ADP801 3.5 0.3 1.0
OE1 B:GLN346 3.6 0.2 1.0
MG B:MG803 3.6 58.4 1.0
NE2 B:GLN346 3.7 0.6 1.0
O1B B:ADP801 3.7 0.5 1.0
NZ B:LYS234 3.9 0.0 1.0
NH1 B:ARG584 4.0 0.4 1.0
NH2 B:ARG584 4.0 0.5 1.0
CD B:GLN346 4.1 0.6 1.0
N B:GLY231 4.1 0.6 1.0
N B:GLY559 4.2 0.1 1.0
CA B:GLY559 4.2 0.6 1.0
NH1 B:ARG381 4.2 0.1 1.0
NH2 B:ARG381 4.4 0.4 1.0
C B:GLY559 4.4 0.4 1.0
CD B:GLU307 4.4 0.5 1.0
CZ B:ARG584 4.5 0.4 1.0
O B:GLY559 4.6 0.9 1.0
O3A B:ADP801 4.6 0.5 1.0
OE1 B:GLU307 4.7 0.6 1.0
CA B:ALA230 4.7 1.0 1.0
O1A B:ADP801 4.8 0.5 1.0
CA B:GLY231 4.8 0.1 1.0
CZ B:ARG381 4.8 0.8 1.0
C B:ALA230 5.0 0.3 1.0

Reference:

S.Dehghani-Tafti, V.Levdikov, A.A.Antson, B.Bax, C.M.Sanders. Structural and Functional Analysis of the Nucleotide and Dna Binding Activities of the Human PIF1 Helicase. Nucleic Acids Res. V. 47 3208 2019.
ISSN: ESSN 1362-4962
PubMed: 30698796
DOI: 10.1093/NAR/GKZ028
Page generated: Sat Dec 12 01:34:25 2020

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