Calcium in PDB 6vza: Crystal Structure of Cytochrome P450 NASF5053 Q65I-A86G Mutant Variant From Streptomyces Sp. Nrrl F-5053 in the Cyclo-L-Trp-L-Pro-Bound State

The structure of Crystal Structure of Cytochrome P450 NASF5053 Q65I-A86G Mutant Variant From Streptomyces Sp. Nrrl F-5053 in the Cyclo-L-Trp-L-Pro-Bound State, PDB code: 6vza was solved by Z.Luo, X.Jia, C.Sun, X.Qu, B.Kobe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.23 / 1.47
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	42.228, 91.310, 93.808, 90.00, 90.00, 90.00
R / Rfree (%)	15.5 / 18

The structure of Crystal Structure of Cytochrome P450 NASF5053 Q65I-A86G Mutant Variant From Streptomyces Sp. Nrrl F-5053 in the Cyclo-L-Trp-L-Pro-Bound State also contains other interesting chemical elements:

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

The binding sites of Calcium atom in the Crystal Structure of Cytochrome P450 NASF5053 Q65I-A86G Mutant Variant From Streptomyces Sp. Nrrl F-5053 in the Cyclo-L-Trp-L-Pro-Bound State (pdb code 6vza). 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 Crystal Structure of Cytochrome P450 NASF5053 Q65I-A86G Mutant Variant From Streptomyces Sp. Nrrl F-5053 in the Cyclo-L-Trp-L-Pro-Bound State, PDB code: 6vza:

Calcium binding site 1 out of 1 in the Crystal Structure of Cytochrome P450 NASF5053 Q65I-A86G Mutant Variant From Streptomyces Sp. Nrrl F-5053 in the Cyclo-L-Trp-L-Pro-Bound State


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 Cytochrome P450 NASF5053 Q65I-A86G Mutant Variant From Streptomyces Sp. Nrrl F-5053 in the Cyclo-L-Trp-L-Pro-Bound State within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca401 b:29.5 occ:1.00 H A:ASP327 2.3 17.9 1.0 HA A:ASP325 2.7 20.5 1.0 HB2 A:ASP327 2.8 19.3 1.0 HD2 A:PRO326 3.0 18.4 1.0 O A:HOH887 3.0 23.5 0.5 N A:ASP327 3.2 14.9 1.0 HB3 A:ASP325 3.2 20.2 1.0 HG23 A:VAL328 3.2 20.5 1.0 C A:ASP325 3.3 16.2 1.0 CA A:ASP325 3.4 17.1 1.0 N A:PRO326 3.5 15.7 1.0 CB A:ASP327 3.6 16.1 1.0 O A:HOH786 3.6 36.6 1.0 CD A:PRO326 3.7 15.3 1.0 O A:ASP325 3.8 14.7 1.0 CA A:ASP327 3.8 16.2 1.0 CB A:ASP325 3.8 16.8 1.0 H A:VAL328 3.9 17.6 1.0 HG2 A:PRO326 3.9 21.1 1.0 C A:ASP327 4.2 16.6 1.0 N A:VAL328 4.2 14.7 1.0 CG2 A:VAL328 4.2 17.1 1.0 C A:PRO326 4.2 15.0 1.0 CG A:ASP327 4.3 27.3 1.0 HB3 A:ASP327 4.3 19.3 1.0 CG A:PRO326 4.4 17.5 1.0 CA A:PRO326 4.4 15.3 1.0 HG21 A:VAL328 4.4 20.5 1.0 HD3 A:PRO326 4.5 18.4 1.0 HB2 A:ASP325 4.5 20.2 1.0 HG22 A:VAL328 4.7 20.5 1.0 N A:ASP325 4.7 17.5 1.0 HA A:ASP327 4.7 19.5 1.0 OD2 A:ASP327 4.7 37.7 1.0 CG A:ASP325 4.8 20.6 1.0 O A:HOH910 4.8 41.1 1.0 OD1 A:ASP325 4.8 23.5 1.0 H A:ASP325 4.8 21.0 1.0 OD1 A:ASP327 4.9 25.3 1.0 O A:ASP327 5.0 18.2 1.0 HB A:VAL328 5.0 17.6 1.0

C.Sun, Z.Luo, W.Zhang, Z.Deng, M.Mobli, B.Kobe, X.Jia, X.Qu. Molecular Basis of Regio- and Stereo-Specificity in Biosynthesis of Bacterial Heterodimeric Diketopiperazines To Be Published.