Aluminium in PDB 5fhh: Structure of Human PIF1 Helicase Domain Residues 200-641

All present enzymatic activity of Structure of Human PIF1 Helicase Domain Residues 200-641:
3.6.4.12;

The structure of Structure of Human PIF1 Helicase Domain Residues 200-641, PDB code: 5fhh was solved by X.Zhou, W.Ren, S.R.Bharath, H.Song, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.06 / 3.60
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	204.750, 204.750, 77.791, 90.00, 90.00, 120.00
R / Rfree (%)	31 / 35.5

The structure of Structure of Human PIF1 Helicase Domain Residues 200-641 also contains other interesting chemical elements:

Fluorine

(F)

8 atoms

The binding sites of Aluminium atom in the Structure of Human PIF1 Helicase Domain Residues 200-641 (pdb code 5fhh). 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 Human PIF1 Helicase Domain Residues 200-641, PDB code: 5fhh:
Jump to Aluminium binding site number: 1; 2;

Aluminium binding site 1 out of 2 in the Structure of Human PIF1 Helicase Domain Residues 200-641


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Structure of Human PIF1 Helicase Domain Residues 200-641 within 5.0Å range: probe atom residue distance (Å) B Occ A:Al702 b:0.7 occ:1.00 AL A:ALF702 0.0 0.7 1.0 F1 A:ALF702 1.8 0.0 1.0 F2 A:ALF702 1.8 0.3 1.0 F4 A:ALF702 1.8 91.6 1.0 F3 A:ALF702 1.8 0.8 1.0 O2B A:ADP701 2.4 75.7 1.0 O1B A:ADP701 2.6 61.0 1.0 PB A:ADP701 2.8 62.1 1.0 NE2 A:GLN346 2.9 51.9 1.0 O3B A:ADP701 3.5 53.7 1.0 CD A:GLN346 3.8 48.5 1.0 OE1 A:GLN346 4.0 52.6 1.0 O3A A:ADP701 4.3 57.1 1.0 N A:GLY559 4.3 76.8 1.0 OG A:SER235 4.4 22.7 1.0 NE2 A:GLN558 4.6 67.4 1.0 CE A:LYS234 4.6 38.7 1.0 CA A:GLY559 4.6 86.7 1.0 NZ A:LYS234 4.8 42.4 1.0

Aluminium binding site 2 out of 2 in the Structure of Human PIF1 Helicase Domain Residues 200-641


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 2 of Structure of Human PIF1 Helicase Domain Residues 200-641 within 5.0Å range: probe atom residue distance (Å) B Occ B:Al702 b:0.8 occ:1.00 AL B:ALF702 0.0 0.8 1.0 F4 B:ALF702 1.8 0.2 1.0 F1 B:ALF702 1.8 0.3 1.0 F3 B:ALF702 1.8 0.3 1.0 F2 B:ALF702 1.8 0.4 1.0 OG B:SER235 1.9 0.9 1.0 O B:GLY233 2.3 0.6 1.0 O1A B:ADP701 2.4 0.3 1.0 O5' B:ADP701 2.9 0.7 1.0 O B:GLY231 2.9 0.2 1.0 C5' B:ADP701 3.0 0.7 1.0 PA B:ADP701 3.2 0.3 1.0 CB B:SER235 3.2 0.0 1.0 C B:GLY233 3.3 1.0 1.0 C B:GLY231 3.5 0.3 1.0 O4' B:ADP701 3.5 0.8 1.0 N B:SER235 3.5 0.7 1.0 O3B B:ADP701 3.5 0.4 1.0 C4' B:ADP701 3.8 0.2 1.0 N B:GLY233 3.8 0.7 1.0 CA B:GLY231 3.9 0.5 1.0 CA B:GLY233 3.9 0.4 1.0 CA B:SER235 3.9 0.1 1.0 N B:GLY231 4.0 0.5 1.0 C8 B:ADP701 4.0 0.2 1.0 O2A B:ADP701 4.2 0.7 1.0 O3A B:ADP701 4.3 0.4 1.0 N B:THR232 4.4 0.9 1.0 N B:LYS234 4.4 0.3 1.0 PB B:ADP701 4.5 0.3 1.0 C B:THR232 4.5 0.3 1.0 CB B:LYS234 4.5 0.0 1.0 C1' B:ADP701 4.6 0.2 1.0 N B:TYR236 4.6 1.0 1.0 C B:LYS234 4.6 0.9 1.0 O2B B:ADP701 4.7 0.2 1.0 N9 B:ADP701 4.7 0.9 1.0 C B:SER235 4.7 0.9 1.0 CA B:LYS234 4.7 0.7 1.0 C3' B:ADP701 4.9 0.6 1.0 CA B:THR232 4.9 0.8 1.0

X.Zhou, W.Ren, S.R.Bharath, X.Tang, Y.He, C.Chen, Z.Liu, D.Li, H.Song. Structural and Functional Insights Into the Unwinding Mechanism of Bacteroides Sp PIF1 Cell Rep V. 14 2030 2016.
ISSN: ESSN 2211-1247
PubMed: 26904952
DOI: 10.1016/J.CELREP.2016.02.008