Sodium in PDB 1ck7: Gelatinase A (Full-Length)

All present enzymatic activity of Gelatinase A (Full-Length):
3.4.24.24;

The structure of Gelatinase A (Full-Length), PDB code: 1ck7 was solved by E.Morgunova, A.Tuuttila, U.Bergmann, M.Isupov, Y.Lindqvist, G.Schneider, K.Tryggvason, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.00 / 2.80
Space group	I 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	121.320, 121.320, 345.110, 90.00, 90.00, 90.00
R / Rfree (%)	28.6 / 32.7

The structure of Gelatinase A (Full-Length) also contains other interesting chemical elements:

Zinc	(Zn)	2 atoms
Calcium	(Ca)	3 atoms
Chlorine	(Cl)	1 atom

The binding sites of Sodium atom in the Gelatinase A (Full-Length) (pdb code 1ck7). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Gelatinase A (Full-Length), PDB code: 1ck7:

Sodium binding site 1 out of 1 in the Gelatinase A (Full-Length)


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Gelatinase A (Full-Length) within 5.0Å range: probe atom residue distance (Å) B Occ A:Na996 b:61.1 occ:1.00 O A:ILE478 2.7 68.3 1.0 O A:ALA571 2.8 76.5 1.0 O A:VAL523 2.9 73.2 1.0 O A:VAL620 2.9 0.7 1.0 CB A:ALA479 3.1 66.0 1.0 CL A:CL995 3.1 58.6 1.0 C A:ALA571 3.8 75.6 1.0 C A:ILE478 3.8 67.5 1.0 C A:VAL523 3.8 69.9 1.0 CA A:ALA479 3.9 76.6 1.0 C A:VAL620 4.1 0.0 1.0 CB A:PHE572 4.2 96.7 1.0 N A:ALA479 4.3 72.1 1.0 N A:VAL620 4.5 0.4 1.0 N A:VAL523 4.5 56.6 1.0 N A:PHE572 4.5 80.0 1.0 CA A:PHE572 4.5 85.0 1.0 N A:ILE478 4.6 60.6 1.0 CA A:VAL523 4.6 64.4 1.0 N A:TYR524 4.6 72.1 1.0 CA A:ALA571 4.6 71.1 1.0 CA A:TYR524 4.7 74.2 1.0 N A:ALA571 4.7 67.7 1.0 CB A:VAL523 4.7 69.7 1.0 CB A:ALA571 4.7 71.7 1.0 CA A:VAL620 4.8 0.0 1.0 CB A:TYR524 4.9 70.6 1.0 CA A:ILE478 4.9 63.6 1.0

E.Morgunova, A.Tuuttila, U.Bergmann, M.Isupov, Y.Lindqvist, G.Schneider, K.Tryggvason. Structure of Human Pro-Matrix Metalloproteinase-2: Activation Mechanism Revealed. Science V. 284 1667 1999.
ISSN: ISSN 0036-8075
PubMed: 10356396
DOI: 10.1126/SCIENCE.284.5420.1667