Calcium in PDB 6b6p: Orthorhombic Trypsin Cryocooled to 100 K with 30% Xylose As Cryoprotectant

All present enzymatic activity of Orthorhombic Trypsin Cryocooled to 100 K with 30% Xylose As Cryoprotectant:
3.4.21.4;

The structure of Orthorhombic Trypsin Cryocooled to 100 K with 30% Xylose As Cryoprotectant, PDB code: 6b6p was solved by D.H.Juers, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	13.38 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.646, 58.315, 66.411, 90.00, 90.00, 90.00
R / Rfree (%)	12.2 / 17.1

The binding sites of Calcium atom in the Orthorhombic Trypsin Cryocooled to 100 K with 30% Xylose As Cryoprotectant (pdb code 6b6p). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Orthorhombic Trypsin Cryocooled to 100 K with 30% Xylose As Cryoprotectant, PDB code: 6b6p:

Calcium binding site 1 out of 1 in the Orthorhombic Trypsin Cryocooled to 100 K with 30% Xylose As Cryoprotectant


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Orthorhombic Trypsin Cryocooled to 100 K with 30% Xylose As Cryoprotectant within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca301 b:5.0 occ:1.00 OE1 A:GLU70 2.2 3.6 1.0 O A:VAL75 2.3 7.2 1.0 OE2 A:GLU80 2.3 5.6 1.0 O A:ASN72 2.4 3.1 1.0 O A:HOH477 2.4 3.5 1.0 O A:HOH408 2.5 3.1 1.0 CD A:GLU70 3.3 7.3 1.0 HG2 A:GLU80 3.3 10.5 1.0 HA A:VAL76 3.3 11.1 1.0 CD A:GLU80 3.3 11.4 1.0 C A:VAL75 3.4 6.2 1.0 H A:GLU77 3.5 6.3 1.0 C A:ASN72 3.5 3.4 1.0 HA A:ILE73 3.5 0.7 1.0 H A:VAL75 3.6 6.5 1.0 HG3 A:GLU80 3.6 10.5 1.0 HG3 A:GLU77 3.7 10.1 1.0 CG A:GLU80 3.7 8.7 1.0 OE2 A:GLU70 3.7 3.5 1.0 H A:ASP71 3.9 4.9 1.0 HA A:GLU70 3.9 5.5 1.0 CA A:VAL76 4.1 9.2 1.0 N A:GLU77 4.2 5.3 1.0 N A:VAL76 4.2 4.6 1.0 HB3 A:ASN72 4.2 8.0 1.0 OE1 A:GLU77 4.2 7.4 1.0 N A:VAL75 4.3 5.4 1.0 CA A:ILE73 4.3 0.5 1.0 N A:ILE73 4.3 2.3 1.0 H A:ASN72 4.3 3.7 1.0 HB2 A:GLU77 4.4 10.8 1.0 N A:ASN72 4.4 3.1 1.0 CA A:VAL75 4.4 2.9 1.0 CA A:ASN72 4.5 2.0 1.0 O A:HOH530 4.5 4.5 1.0 CG A:GLU77 4.5 8.4 1.0 OE1 A:GLU80 4.5 5.4 1.0 HB3 A:GLU70 4.6 5.2 1.0 C A:ILE73 4.6 8.9 1.0 CG A:GLU70 4.6 2.6 1.0 N A:ASP71 4.6 4.1 1.0 C A:VAL76 4.6 11.7 1.0 HB A:VAL75 4.7 8.0 1.0 O A:HOH608 4.7 7.5 1.0 CA A:GLU70 4.7 4.6 1.0 CD A:GLU77 4.8 23.3 1.0 HZ A:PHE82 4.8 5.2 1.0 CB A:ASN72 4.9 6.7 1.0 CB A:GLU70 4.9 4.3 1.0 CB A:GLU77 4.9 9.0 1.0 N A:ASN74 4.9 3.9 1.0 HG22 A:VAL76 4.9 6.7 1.0 O A:ILE73 4.9 5.2 1.0 HG2 A:GLU70 5.0 3.2 1.0 H A:VAL76 5.0 5.5 1.0 H A:ASN74 5.0 4.6 1.0 C A:ASP71 5.0 3.0 1.0

D.H.Juers, C.A.Farley, C.P.Saxby, R.A.Cotter, J.K.B.Cahn, R.C.Holton-Burke, K.Harrison, Z.Wu. The Impact of Cryosolution Thermal Contraction on Proteins and Protein Crystals: Volumes, Conformation and Order. Acta Crystallogr D Struct V. 74 922 2018BIOL.
ISSN: ISSN 2059-7983
PubMed: 30198901
DOI: 10.1107/S2059798318008793