Calcium in PDB 5ze3: Crystal Structure of Human Lysyl Oxidase-Like 2 (HLOXL2) in A Precursor State

All present enzymatic activity of Crystal Structure of Human Lysyl Oxidase-Like 2 (HLOXL2) in A Precursor State:
1.4.3.13;

The structure of Crystal Structure of Human Lysyl Oxidase-Like 2 (HLOXL2) in A Precursor State, PDB code: 5ze3 was solved by X.Zhang, M.Liu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.50 / 2.40
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	73.095, 61.487, 137.883, 90.00, 102.33, 90.00
R / Rfree (%)	21.7 / 23.9

The structure of Crystal Structure of Human Lysyl Oxidase-Like 2 (HLOXL2) in A Precursor State also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Calcium atom in the Crystal Structure of Human Lysyl Oxidase-Like 2 (HLOXL2) in A Precursor State (pdb code 5ze3). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of Human Lysyl Oxidase-Like 2 (HLOXL2) in A Precursor State, PDB code: 5ze3:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of Human Lysyl Oxidase-Like 2 (HLOXL2) in A Precursor State


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Human Lysyl Oxidase-Like 2 (HLOXL2) in A Precursor State within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca801 b:28.9 occ:1.00 OD1 A:ASN727 2.3 46.8 1.0 OD1 A:ASN728 2.3 32.5 1.0 OD1 A:ASP549 2.3 21.5 1.0 O A:ASP724 2.4 24.0 1.0 O A:LEU550 2.5 25.7 1.0 OE1 A:GLU722 2.6 19.8 1.0 CG A:ASN727 3.2 33.0 1.0 CG A:ASN728 3.4 33.8 1.0 N A:LEU550 3.4 21.8 1.0 C A:LEU550 3.5 25.0 1.0 CG A:ASP549 3.5 28.2 1.0 C A:ASP724 3.5 18.4 1.0 ND2 A:ASN727 3.6 30.6 1.0 CD A:GLU722 3.8 30.2 1.0 ND2 A:ASN728 3.9 29.5 1.0 C A:ASP549 4.0 24.9 1.0 CA A:LEU550 4.0 21.9 1.0 CA A:ASP549 4.2 22.6 1.0 OD2 A:ASP549 4.4 37.2 1.0 CB A:ASP549 4.4 30.3 1.0 N A:TYR725 4.4 24.7 1.0 N A:ASN728 4.4 15.5 1.0 CA A:TYR725 4.5 18.2 1.0 CA A:ASP724 4.5 21.3 1.0 CB A:ASP724 4.5 23.2 1.0 C A:ASN727 4.5 32.2 1.0 CB A:LEU550 4.5 12.2 1.0 CB A:ASN727 4.6 16.7 1.0 OE2 A:GLU722 4.6 28.9 1.0 CB A:GLU722 4.6 21.6 1.0 CB A:ASN728 4.6 17.0 1.0 N A:VAL551 4.7 16.5 1.0 N A:ASN727 4.7 32.4 1.0 CA A:ASN728 4.7 14.1 1.0 CA A:ASN727 4.8 35.4 1.0 O A:ASP549 4.8 18.6 1.0 N A:ASP724 4.8 25.5 1.0 CG A:GLU722 4.8 25.4 1.0 O A:ASN727 4.9 24.5 1.0 C A:TYR725 5.0 20.1 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of Human Lysyl Oxidase-Like 2 (HLOXL2) in A Precursor State


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of Human Lysyl Oxidase-Like 2 (HLOXL2) in A Precursor State within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca801 b:40.8 occ:1.00 OD1 B:ASP549 2.1 52.1 1.0 OD1 B:ASN728 2.1 47.4 1.0 OE1 B:GLU722 2.2 46.1 1.0 O B:ASP724 2.4 64.9 1.0 OD1 B:ASN727 2.4 53.4 1.0 O B:LEU550 2.6 50.0 1.0 N B:LEU550 3.2 50.8 1.0 CD B:GLU722 3.2 57.9 1.0 CG B:ASN728 3.3 47.8 1.0 CG B:ASN727 3.4 55.8 1.0 CG B:ASP549 3.4 49.6 1.0 C B:LEU550 3.6 53.9 1.0 C B:ASP724 3.6 49.0 1.0 ND2 B:ASN727 3.7 52.1 1.0 OE2 B:GLU722 3.7 64.0 1.0 ND2 B:ASN728 3.8 47.7 1.0 CA B:LEU550 3.9 53.7 1.0 C B:ASP549 4.0 55.0 1.0 CA B:ASP549 4.1 49.3 1.0 OD2 B:ASP549 4.2 50.4 1.0 CB B:ASP549 4.3 49.6 1.0 CG B:GLU722 4.4 45.5 1.0 CA B:TYR725 4.4 47.4 1.0 N B:ASN728 4.4 50.1 1.0 N B:TYR725 4.5 46.1 1.0 CB B:LEU550 4.5 50.2 1.0 CB B:ASN728 4.5 48.8 1.0 CB B:GLU722 4.6 45.1 1.0 CA B:ASP724 4.6 51.1 1.0 C B:ASN727 4.7 49.4 1.0 CB B:ASN727 4.7 48.9 1.0 CA B:ASN728 4.7 51.5 1.0 N B:ASP724 4.8 52.0 1.0 N B:VAL551 4.8 51.5 1.0 CB B:ASP724 4.8 45.8 1.0 N B:ASN727 4.9 59.8 1.0 O B:ASP549 5.0 51.0 1.0

X.Zhang, Q.Wang, J.Wu, J.Wang, Y.Shi, M.Liu. Crystal Structure of Human Lysyl Oxidase-Like 2 (HLOXL2) in A Precursor State. Proc. Natl. Acad. Sci. V. 115 3828 2018U.S.A..
ISSN: ESSN 1091-6490
PubMed: 29581294
DOI: 10.1073/PNAS.1720859115