Calcium in PDB 7r6b: Crystal Structure of Mutant R43D/L124D/R125A/C273S of L-Asparaginase I From Yersinia Pestis

All present enzymatic activity of Crystal Structure of Mutant R43D/L124D/R125A/C273S of L-Asparaginase I From Yersinia Pestis:
3.5.1.1;

The structure of Crystal Structure of Mutant R43D/L124D/R125A/C273S of L-Asparaginase I From Yersinia Pestis, PDB code: 7r6b was solved by P.Strzelczyk, A.Wlodawer, J.Lubkowski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.85 / 2.03
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	100.263, 115.893, 127.548, 90, 90, 90
R / Rfree (%)	17 / 21.8

The binding sites of Calcium atom in the Crystal Structure of Mutant R43D/L124D/R125A/C273S of L-Asparaginase I From Yersinia Pestis (pdb code 7r6b). 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 Mutant R43D/L124D/R125A/C273S of L-Asparaginase I From Yersinia Pestis, PDB code: 7r6b:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of Mutant R43D/L124D/R125A/C273S of L-Asparaginase I From Yersinia Pestis


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 Mutant R43D/L124D/R125A/C273S of L-Asparaginase I From Yersinia Pestis within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca407 b:25.3 occ:1.00 OE1 B:GLU321 2.4 22.4 1.0 O B:HOH658 2.4 35.8 1.0 OE2 B:GLU321 2.5 17.4 1.0 CD B:GLU321 2.7 20.1 1.0 CG B:GLU321 4.3 21.9 1.0 N B:SER318 4.6 21.1 1.0 O B:SER316 4.8 18.0 1.0 CA B:LEU317 4.8 18.1 1.0 CB B:SER318 5.0 20.9 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of Mutant R43D/L124D/R125A/C273S of L-Asparaginase I From Yersinia Pestis


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 Mutant R43D/L124D/R125A/C273S of L-Asparaginase I From Yersinia Pestis within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca408 b:66.4 occ:1.00 NE2 B:HIS70 3.2 37.8 1.0 NE2 B:HIS52 3.6 31.9 1.0 CD1 B:TYR54 3.7 24.5 1.0 CE1 B:TYR54 3.7 23.7 1.0 CG B:TYR54 3.9 21.7 1.0 CZ B:TYR54 3.9 24.8 1.0 CD2 B:HIS70 4.0 38.5 1.0 CD2 B:TYR54 4.1 24.3 1.0 CE2 B:TYR54 4.1 22.0 1.0 CD2 B:HIS52 4.1 32.5 1.0 CE1 B:HIS70 4.2 38.4 1.0 OH B:TYR54 4.6 22.5 1.0 O B:HOH584 4.6 23.9 1.0 CB B:TYR54 4.7 23.5 1.0 CA B:TYR54 4.7 26.0 1.0 CG B:ASP74 4.8 20.8 1.0 CE1 B:HIS52 4.8 33.6 1.0 O B:HOH505 4.8 30.1 1.0 OD1 B:ASP74 4.9 23.0 1.0 OD2 B:ASP74 5.0 23.1 1.0

P.Strzelczyk, D.Zhang, J.Alexandratos, G.Piszczek, A.Wlodawer, J.Lubkowski. The Dimeric Form of Bacterial L-Asparaginase Ypai Is Fully Active. Febs J. 2022.
ISSN: ISSN 1742-464X
PubMed: 36152020
DOI: 10.1111/FEBS.16635