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Iron 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

Protein crystallography data

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

Other elements in 6vza:

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:

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

Iron Binding Sites:

The binding sites of Iron 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 Iron atom.
In total only one binding site of Iron 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:

Iron binding site 1 out of 1 in 6vza

Go back to Iron Binding Sites List in 6vza
Iron 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 Iron with other atoms in the Fe 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:Fe405

b:11.2
occ:1.00
FE A:HEM405 0.0 11.2 1.0
NB A:HEM405 2.0 10.2 1.0
NC A:HEM405 2.0 8.8 1.0
NA A:HEM405 2.0 9.3 1.0
ND A:HEM405 2.1 11.5 1.0
SG A:CYS348 2.4 11.9 1.0
O A:HOH625 2.8 16.7 1.0
C4B A:HEM405 3.0 10.2 1.0
C4C A:HEM405 3.1 11.9 1.0
C1B A:HEM405 3.1 9.3 1.0
C1C A:HEM405 3.1 9.8 1.0
C4D A:HEM405 3.1 10.5 1.0
C4A A:HEM405 3.1 10.9 1.0
C1D A:HEM405 3.1 9.5 1.0
C1A A:HEM405 3.1 9.5 1.0
HB2 A:CYS348 3.2 11.7 1.0
CB A:CYS348 3.4 9.8 1.0
CHC A:HEM405 3.4 10.3 1.0
CHD A:HEM405 3.4 11.8 1.0
CHA A:HEM405 3.4 9.2 1.0
CHB A:HEM405 3.4 11.2 1.0
HA A:CYS348 3.8 11.7 1.0
H A:GLY350 3.8 11.8 1.0
HD2 A:PRO349 4.1 13.2 1.0
CA A:CYS348 4.1 9.8 1.0
HA3 A:GLY350 4.2 11.6 1.0
HB3 A:CYS348 4.2 11.7 1.0
C3C A:HEM405 4.3 10.2 1.0
C2B A:HEM405 4.3 11.0 1.0
C3B A:HEM405 4.3 12.4 1.0
O A:ALA237 4.3 12.7 1.0
C3A A:HEM405 4.3 9.8 1.0
C2C A:HEM405 4.3 10.2 1.0
C2D A:HEM405 4.3 11.2 1.0
C2A A:HEM405 4.3 9.7 1.0
C3D A:HEM405 4.3 11.6 1.0
HZ3 A:QRP406 4.3 17.2 1.0
HHC A:HEM405 4.4 12.3 1.0
HHD A:HEM405 4.4 14.2 1.0
HHA A:HEM405 4.4 11.0 1.0
HHB A:HEM405 4.4 13.5 1.0
HB1 A:ALA237 4.5 17.4 1.0
HD1 A:PHE341 4.5 11.5 1.0
HH2 A:QRP406 4.5 15.2 1.0
N A:GLY350 4.6 9.8 1.0
HG21 A:THR241 4.7 17.1 1.0
HG1 A:THR241 4.8 14.2 1.0
CZ3 A:QRP406 4.8 14.3 1.0
CA A:GLY350 4.8 9.7 1.0
C A:CYS348 4.8 11.3 1.0
HNE1 A:QRP407 4.8 15.2 1.0
CH2 A:QRP406 4.9 12.7 1.0
CD A:PRO349 5.0 11.0 1.0

Reference:

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.
Page generated: Wed Aug 7 13:45:03 2024

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