Aluminium in PDB 1khj: E. Coli Alkaline Phosphatase Mutant (D153HD330N) Mimic of the Transition States with Aluminium Fluoride

All present enzymatic activity of E. Coli Alkaline Phosphatase Mutant (D153HD330N) Mimic of the Transition States with Aluminium Fluoride:
3.1.3.1;

The structure of E. Coli Alkaline Phosphatase Mutant (D153HD330N) Mimic of the Transition States with Aluminium Fluoride, PDB code: 1khj was solved by M.H.Le Du, C.Lamoure, B.H.Muller, O.V.Bulgakov, E.Lajeunesse, A.Menez, J.C.Boulain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.30
Space group	P 63 2 2
Cell size a, b, c (Å), α, β, γ (°)	163.511, 163.511, 138.025, 90.00, 90.00, 120.00
R / Rfree (%)	18 / 22.3

The structure of E. Coli Alkaline Phosphatase Mutant (D153HD330N) Mimic of the Transition States with Aluminium Fluoride also contains other interesting chemical elements:

Fluorine	(F)	6 atoms
Zinc	(Zn)	4 atoms

The binding sites of Aluminium atom in the E. Coli Alkaline Phosphatase Mutant (D153HD330N) Mimic of the Transition States with Aluminium Fluoride (pdb code 1khj). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total 2 binding sites of Aluminium where determined in the E. Coli Alkaline Phosphatase Mutant (D153HD330N) Mimic of the Transition States with Aluminium Fluoride, PDB code: 1khj:
Jump to Aluminium binding site number: 1; 2;

Aluminium binding site 1 out of 2 in the E. Coli Alkaline Phosphatase Mutant (D153HD330N) Mimic of the Transition States with Aluminium Fluoride


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of E. Coli Alkaline Phosphatase Mutant (D153HD330N) Mimic of the Transition States with Aluminium Fluoride within 5.0Å range: probe atom residue distance (Å) B Occ A:Al453 b:37.3 occ:1.00 AL A:AF3453 0.0 37.3 1.0 F2 A:AF3453 1.5 38.8 1.0 F3 A:AF3453 1.5 34.6 1.0 OG A:SER102 1.6 24.4 1.0 F1 A:AF3453 1.7 31.9 1.0 O A:HOH1003 1.8 32.1 1.0 CB A:SER102 3.0 14.5 1.0 O A:HOH1001 3.0 27.2 1.0 ZN A:ZN450 3.3 23.1 1.0 N A:SER102 3.5 12.9 1.0 O A:HOH1002 3.5 43.0 1.0 NH2 A:ARG166 3.6 36.2 1.0 ZN A:ZN451 3.6 27.1 1.0 CE1 A:HIS412 3.7 12.1 1.0 NH1 A:ARG166 3.8 39.7 1.0 CA A:SER102 3.8 15.2 1.0 NE2 A:HIS412 3.9 12.0 1.0 CZ A:ARG166 4.1 40.0 1.0 OD2 A:ASP327 4.3 15.7 1.0 CE1 A:HIS153 4.5 20.3 1.0 O A:HOH1388 4.5 47.2 1.0 C A:ASP101 4.6 10.0 1.0 OD1 A:ASP327 4.7 20.2 1.0 NE2 A:HIS370 4.7 13.0 1.0 CG A:ASP327 4.8 17.9 1.0 OD2 A:ASP51 4.8 24.9 1.0 NE2 A:HIS331 4.9 11.4 1.0 NE2 A:HIS153 4.9 19.2 1.0 CA A:ASP101 4.9 11.2 1.0 ND1 A:HIS412 5.0 16.0 1.0 CB A:ASP101 5.0 14.0 1.0

Aluminium binding site 2 out of 2 in the E. Coli Alkaline Phosphatase Mutant (D153HD330N) Mimic of the Transition States with Aluminium Fluoride


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 2 of E. Coli Alkaline Phosphatase Mutant (D153HD330N) Mimic of the Transition States with Aluminium Fluoride within 5.0Å range: probe atom residue distance (Å) B Occ B:Al453 b:41.9 occ:1.00 AL B:AF3453 0.0 41.9 1.0 F3 B:AF3453 1.4 40.7 1.0 F2 B:AF3453 1.5 39.1 1.0 F1 B:AF3453 1.6 35.4 1.0 OG B:SER102 1.8 21.7 1.0 O B:HOH1006 1.9 35.7 1.0 O B:HOH1004 2.8 30.7 1.0 CB B:SER102 3.2 14.8 1.0 NH2 B:ARG166 3.3 40.2 1.0 ZN B:ZN450 3.3 20.4 1.0 N B:SER102 3.6 13.4 1.0 NH1 B:ARG166 3.7 42.8 1.0 CE1 B:HIS412 3.7 16.5 1.0 ZN B:ZN451 3.9 26.8 1.0 CZ B:ARG166 4.0 44.0 1.0 O B:HOH1005 4.0 37.5 1.0 CA B:SER102 4.0 12.5 1.0 NE2 B:HIS412 4.1 17.3 1.0 OD2 B:ASP327 4.4 19.4 1.0 CE1 B:HIS153 4.4 16.1 1.0 C B:ASP101 4.6 11.7 1.0 NE2 B:HIS370 4.7 17.1 1.0 NE2 B:HIS331 4.8 10.7 1.0 CB B:ASP101 4.8 14.3 1.0 CA B:ASP101 4.9 11.1 1.0 OD1 B:ASP327 4.9 20.1 1.0 NE2 B:HIS153 4.9 17.0 1.0 CG B:ASP327 4.9 16.4 1.0 ND1 B:HIS412 5.0 17.6 1.0

M.H.Le Du, C.Lamoure, B.H.Muller, O.V.Bulgakov, E.Lajeunesse, A.Menez, J.C.Boulain. Artificial Evolution of An Enzyme Active Site: Structural Studies of Three Highly Active Mutants of Escherichia Coli Alkaline Phosphatase. J.Mol.Biol. V. 316 941 2002.
ISSN: ISSN 0022-2836
PubMed: 11884134
DOI: 10.1006/JMBI.2001.5384