Calcium in PDB 4us6: New Crystal Form of Glucose Isomerase Grown in Short Peptide Supramolecular Hydrogels

All present enzymatic activity of New Crystal Form of Glucose Isomerase Grown in Short Peptide Supramolecular Hydrogels:
5.3.1.5;

The structure of New Crystal Form of Glucose Isomerase Grown in Short Peptide Supramolecular Hydrogels, PDB code: 4us6 was solved by J.A.Gavira, M.Conejero-Muriel, J.J.Diaz-Mochon, L.Alvarez De Cienfuegos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	99.21 / 1.20
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	85.999, 93.677, 99.215, 90.00, 90.00, 90.00
R / Rfree (%)	10.648 / 13.237

The structure of New Crystal Form of Glucose Isomerase Grown in Short Peptide Supramolecular Hydrogels also contains other interesting chemical elements:

Magnesium	(Mg)	3 atoms
Sodium	(Na)	2 atoms

The binding sites of Calcium atom in the New Crystal Form of Glucose Isomerase Grown in Short Peptide Supramolecular Hydrogels (pdb code 4us6). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the New Crystal Form of Glucose Isomerase Grown in Short Peptide Supramolecular Hydrogels, PDB code: 4us6:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the New Crystal Form of Glucose Isomerase Grown in Short Peptide Supramolecular Hydrogels


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of New Crystal Form of Glucose Isomerase Grown in Short Peptide Supramolecular Hydrogels within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1388 b:7.0 occ:1.00 HE2 A:HIS220 1.7 7.5 1.0 OE2 A:GLU217 2.0 7.1 1.0 O A:HOH2333 2.2 9.8 1.0 OD1 A:ASP257 2.2 7.7 1.0 OD2 A:ASP255 2.2 8.9 1.0 OD1 A:ASP255 2.3 7.4 1.0 NE2 A:HIS220 2.4 8.1 1.0 CG A:ASP255 2.6 8.2 1.0 CD A:GLU217 2.9 6.5 1.0 CD2 A:HIS220 3.1 7.1 1.0 CG A:ASP257 3.1 8.5 1.0 HD2 A:HIS220 3.2 6.9 1.0 OE1 A:GLU217 3.2 7.5 1.0 HD22 A:ASN247 3.3 6.5 1.0 CE1 A:HIS220 3.4 7.8 1.0 OD2 A:ASP257 3.4 11.5 1.0 HE1 A:HIS220 3.6 7.8 1.0 O A:HOH2307 3.7 15.3 1.0 HD21 A:ASN247 3.9 6.4 1.0 O A:HOH2373 4.0 28.8 1.0 ND2 A:ASN247 4.0 6.5 1.0 HE3 A:LYS183 4.0 7.8 1.0 HO1 A:GOL1390 4.0 8.7 1.0 O A:HOH2364 4.1 7.5 1.0 CB A:ASP255 4.1 7.8 1.0 CG A:HIS220 4.3 6.6 1.0 O3 A:GOL1390 4.3 8.4 1.0 CG A:GLU217 4.3 6.5 1.0 HG2 A:GLU217 4.3 6.2 1.0 ND1 A:HIS220 4.4 7.6 1.0 HZ3 A:LYS183 4.4 11.7 1.0 HB2 A:ASP255 4.4 8.2 1.0 HB3 A:ASP255 4.4 8.0 1.0 OD2 A:ASP287 4.4 8.2 1.0 CB A:ASP257 4.5 8.0 1.0 HO3 A:GOL1392 4.5 23.3 1.0 HA A:ASP257 4.5 7.4 1.0 H A:ASP257 4.6 6.9 1.0 O A:HOH2372 4.7 25.5 1.0 O1 A:GOL1392 4.7 26.3 1.0 MG A:MG1389 4.7 6.4 1.0 HG3 A:GLU217 4.8 6.4 1.0 CE A:LYS183 4.9 7.1 1.0 CA A:ASP257 4.9 6.9 1.0 HD2 A:LYS183 5.0 6.9 1.0 N A:ASP257 5.0 6.6 1.0 HA A:ASP255 5.0 6.8 1.0 HZ1 A:LYS289 5.0 13.3 0.6

Calcium binding site 2 out of 2 in the New Crystal Form of Glucose Isomerase Grown in Short Peptide Supramolecular Hydrogels


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of New Crystal Form of Glucose Isomerase Grown in Short Peptide Supramolecular Hydrogels within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca1389 b:7.0 occ:1.00 HE2 B:HIS220 1.7 6.6 1.0 OE2 B:GLU217 2.1 6.5 1.0 O B:HOH2283 2.2 10.2 1.0 OD1 B:ASP257 2.2 8.0 1.0 OD2 B:ASP255 2.2 10.3 1.0 OD1 B:ASP255 2.3 7.6 1.0 NE2 B:HIS220 2.3 7.2 1.0 CG B:ASP255 2.6 7.4 1.0 CD B:GLU217 3.0 6.1 1.0 CD2 B:HIS220 3.1 6.4 1.0 CG B:ASP257 3.1 7.7 1.0 HD2 B:HIS220 3.1 6.3 1.0 OE1 B:GLU217 3.2 7.5 1.0 HD22 B:ASN247 3.3 6.1 1.0 OD2 B:ASP257 3.3 11.2 1.0 CE1 B:HIS220 3.4 6.8 1.0 HE1 B:HIS220 3.6 6.7 1.0 O B:HOH2267 3.7 17.0 1.0 HO3 B:GOL1391 3.9 7.8 0.0 HD21 B:ASN247 4.0 5.8 1.0 ND2 B:ASN247 4.0 6.2 1.0 O B:HOH2304 4.0 6.6 1.0 HE3 B:LYS183 4.1 8.0 1.0 CB B:ASP255 4.1 7.4 1.0 CG B:HIS220 4.2 6.0 1.0 HZ3 B:LYS183 4.3 12.6 1.0 O1 B:GOL1391 4.3 8.2 1.0 CG B:GLU217 4.3 6.3 1.0 ND1 B:HIS220 4.4 6.9 1.0 HG2 B:GLU217 4.4 6.5 1.0 HB2 B:ASP255 4.4 7.4 1.0 HB3 B:ASP255 4.4 7.7 1.0 OD2 B:ASP287 4.5 7.8 1.0 HO3 B:GOL1392 4.5 18.9 0.6 CB B:ASP257 4.5 7.4 1.0 H B:ASP257 4.6 6.7 1.0 HA B:ASP257 4.6 6.4 1.0 O B:HOH2310 4.6 26.6 1.0 O1 B:GOL1392 4.7 18.1 0.6 MG B:MG1390 4.7 6.2 1.0 HO3 B:GOL1392 4.8 18.1 0.4 HG3 B:GLU217 4.9 6.3 1.0 CE B:LYS183 4.9 7.5 1.0 HD2 B:LYS183 4.9 7.1 1.0 O1 B:GOL1392 4.9 22.4 0.4 HO2 B:GOL1392 4.9 41.1 0.4 NZ B:LYS183 4.9 12.4 1.0 CA B:ASP257 4.9 6.1 1.0 HZ1 B:LYS289 5.0 13.5 0.5 HA B:ASP255 5.0 7.0 1.0 N B:ASP257 5.0 6.4 1.0 HZ2 B:LYS183 5.0 10.9 1.0

M.Conejero-Muriel, J.A.Gavira, E.Pineda-Molina, A.Belsom, M.Bradley, M.Moral, J.D.D.Garcia-Lopez Duran, A.Luque Gonzalez, J.J.Diaz-Mochon, R.Contreras-Montoya, A.Martinez-Peragon, J.M.Cuerva, L.Alvarez De Cienfuegos. Influence of the Chirality of Short Peptide Supramolecular Hydrogels in Protein Crystallogenesis. Chem.Commun.(Camb.) V. 51 3862 2015.
ISSN: ISSN 1359-7345
PubMed: 25655841
DOI: 10.1039/C4CC09024A