Calcium in PDB 7vo7: Crystal Structure of Trypsin in Complex with Lima Bean Trypsin Inhibitor at 2.25A Resolution.

All present enzymatic activity of Crystal Structure of Trypsin in Complex with Lima Bean Trypsin Inhibitor at 2.25A Resolution.:
3.4.21.4;

The structure of Crystal Structure of Trypsin in Complex with Lima Bean Trypsin Inhibitor at 2.25A Resolution., PDB code: 7vo7 was solved by M.S.Ahmad, Z.Akbar, M.I.Choudhary, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	17.91 / 2.25
Space group	P 41
Cell size a, b, c (Å), α, β, γ (°)	54.009, 54.009, 179.817, 90, 90, 90
R / Rfree (%)	18.1 / 23.3

The structure of Crystal Structure of Trypsin in Complex with Lima Bean Trypsin Inhibitor at 2.25A Resolution. also contains other interesting chemical elements:

Chlorine	(Cl)	2 atoms
Sodium	(Na)	1 atom

The binding sites of Calcium atom in the Crystal Structure of Trypsin in Complex with Lima Bean Trypsin Inhibitor at 2.25A Resolution. (pdb code 7vo7). 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 Trypsin in Complex with Lima Bean Trypsin Inhibitor at 2.25A Resolution., PDB code: 7vo7:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of Trypsin in Complex with Lima Bean Trypsin Inhibitor at 2.25A Resolution.


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 Trypsin in Complex with Lima Bean Trypsin Inhibitor at 2.25A Resolution. within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca305 b:13.5 occ:1.00 OE1 A:GLU70 2.3 10.7 1.0 O A:VAL75 2.3 15.4 1.0 O A:ASN72 2.4 17.1 1.0 O A:HOH439 2.4 11.5 1.0 OE2 A:GLU80 2.5 13.2 1.0 O A:HOH406 2.5 13.8 1.0 CD A:GLU70 3.4 11.8 1.0 CD A:GLU80 3.4 19.0 1.0 C A:VAL75 3.4 14.8 1.0 C A:ASN72 3.5 13.0 1.0 CG A:GLU80 3.5 16.4 1.0 OE2 A:GLU70 3.8 13.2 1.0 OE1 A:GLU77 3.9 19.4 1.0 CA A:VAL76 4.0 18.1 1.0 N A:GLU77 4.0 17.7 1.0 N A:VAL76 4.1 16.0 1.0 CA A:ILE73 4.2 18.4 1.0 O A:HOH421 4.2 16.2 1.0 N A:VAL75 4.3 16.6 1.0 N A:ILE73 4.3 16.2 1.0 N A:ASN72 4.4 10.9 1.0 CA A:ASN72 4.4 13.8 1.0 N A:ASP71 4.5 13.4 1.0 CA A:VAL75 4.5 17.2 1.0 C A:ILE73 4.5 16.1 1.0 C A:VAL76 4.5 19.2 1.0 CG A:GLU77 4.5 15.4 1.0 OE1 A:GLU80 4.5 14.0 1.0 O A:HOH471 4.6 22.8 1.0 CG A:GLU70 4.6 11.2 1.0 CD A:GLU77 4.7 21.0 1.0 CB A:GLU77 4.7 17.8 1.0 CA A:GLU70 4.7 14.3 1.0 O A:ILE73 4.8 16.9 1.0 CB A:GLU70 4.8 12.2 1.0 CB A:ASN72 4.8 19.0 1.0 N A:ASN74 4.9 13.8 1.0 C A:ASP71 5.0 12.6 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of Trypsin in Complex with Lima Bean Trypsin Inhibitor at 2.25A Resolution.


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 Trypsin in Complex with Lima Bean Trypsin Inhibitor at 2.25A Resolution. within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca303 b:15.3 occ:1.00 OE1 B:GLU70 2.3 13.0 1.0 O B:VAL75 2.4 18.8 1.0 O B:HOH402 2.4 11.6 1.0 O B:ASN72 2.4 13.9 1.0 O B:HOH419 2.4 16.1 1.0 OE2 B:GLU80 2.4 11.5 1.0 CD B:GLU70 3.3 14.0 1.0 CD B:GLU80 3.3 18.6 1.0 C B:VAL75 3.5 14.6 1.0 CG B:GLU80 3.5 15.4 1.0 C B:ASN72 3.5 13.1 1.0 OE2 B:GLU70 3.7 14.4 1.0 OE1 B:GLU77 4.0 21.2 1.0 CA B:VAL76 4.1 17.8 1.0 N B:GLU77 4.1 17.1 1.0 N B:VAL76 4.2 16.9 1.0 CA B:ILE73 4.3 19.6 1.0 N B:VAL75 4.3 16.7 1.0 N B:ILE73 4.3 14.3 1.0 O B:HOH490 4.4 14.0 1.0 N B:ASN72 4.4 14.3 1.0 CA B:ASN72 4.5 16.5 1.0 CA B:VAL75 4.5 17.5 1.0 OE1 B:GLU80 4.5 11.8 1.0 CG B:GLU70 4.6 12.4 1.0 N B:ASP71 4.6 11.6 1.0 C B:ILE73 4.6 16.6 1.0 C B:VAL76 4.6 18.8 1.0 CG B:GLU77 4.7 15.6 1.0 CB B:GLU77 4.7 13.6 1.0 CA B:GLU70 4.7 15.2 1.0 CD B:GLU77 4.8 17.8 1.0 CB B:GLU70 4.8 11.9 1.0 N B:ASN74 4.9 14.6 1.0 CB B:ASN72 4.9 18.8 1.0 CB B:GLU80 5.0 15.5 1.0

M.S.Ahmad, Z.Akbar, M.I.Choudhary. Insight Into the Structural Basis of the Dual Inhibitory Mode of Lima Bean (Phaseolus Lunatus) Serine Protease Inhibitor. Proteins V. 91 22 2023.
ISSN: ESSN 1097-0134
PubMed: 35927030
DOI: 10.1002/PROT.26407