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Iron in PDB 6vby: Cinnamate 4-Hydroxylase (C4H1) From Sorghum Bicolor

Enzymatic activity of Cinnamate 4-Hydroxylase (C4H1) From Sorghum Bicolor

All present enzymatic activity of Cinnamate 4-Hydroxylase (C4H1) From Sorghum Bicolor:
1.14.13.11;

Protein crystallography data

The structure of Cinnamate 4-Hydroxylase (C4H1) From Sorghum Bicolor, PDB code: 6vby was solved by B.Zhang, C.Kang, K.M.Lewis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 65.28 / 1.70
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 132.278, 132.278, 79.431, 90.00, 90.00, 120.00
R / Rfree (%) 19.9 / 21.5

Iron Binding Sites:

The binding sites of Iron atom in the Cinnamate 4-Hydroxylase (C4H1) From Sorghum Bicolor (pdb code 6vby). 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 Cinnamate 4-Hydroxylase (C4H1) From Sorghum Bicolor, PDB code: 6vby:

Iron binding site 1 out of 1 in 6vby

Go back to Iron Binding Sites List in 6vby
Iron binding site 1 out of 1 in the Cinnamate 4-Hydroxylase (C4H1) From Sorghum Bicolor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cinnamate 4-Hydroxylase (C4H1) From Sorghum Bicolor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe602

b:11.8
occ:1.00
FE A:HEM602 0.0 11.8 1.0
NC A:HEM602 2.0 12.0 1.0
ND A:HEM602 2.0 10.9 1.0
NB A:HEM602 2.0 11.9 1.0
NA A:HEM602 2.0 11.3 1.0
O8 A:EPE601 2.3 13.8 1.0
HO8 A:EPE601 2.5 16.7 1.0
SG A:CYS443 2.5 14.5 1.0
H81 A:EPE601 2.9 17.8 1.0
C4C A:HEM602 3.0 10.9 1.0
C1C A:HEM602 3.0 11.1 1.0
C1D A:HEM602 3.0 11.5 1.0
C4B A:HEM602 3.0 11.3 1.0
C1A A:HEM602 3.1 11.6 1.0
C4D A:HEM602 3.1 10.4 1.0
C1B A:HEM602 3.1 12.3 1.0
C4A A:HEM602 3.1 11.2 1.0
HB2 A:CYS443 3.1 16.6 1.0
C8 A:EPE601 3.1 14.8 1.0
CB A:CYS443 3.4 14.5 1.0
CHD A:HEM602 3.4 9.8 1.0
CHC A:HEM602 3.4 10.4 1.0
CHA A:HEM602 3.4 12.6 1.0
CHB A:HEM602 3.4 11.7 1.0
H71 A:EPE601 3.6 17.6 1.0
H82 A:EPE601 3.8 17.8 1.0
HA A:CYS443 3.9 17.8 1.0
C7 A:EPE601 3.9 14.6 1.0
HB1 A:ALA302 4.1 15.2 1.0
H A:GLY445 4.1 14.9 1.0
HB3 A:CYS443 4.1 16.6 1.0
HD2 A:PRO444 4.2 16.3 1.0
CA A:CYS443 4.2 15.2 1.0
O A:ALA302 4.2 13.1 1.0
C3C A:HEM602 4.2 10.3 1.0
C2C A:HEM602 4.2 10.7 1.0
HD1 A:PHE436 4.3 15.6 1.0
C2D A:HEM602 4.3 13.3 1.0
C2A A:HEM602 4.3 10.4 1.0
C3D A:HEM602 4.3 11.2 1.0
C3B A:HEM602 4.3 13.2 1.0
C2B A:HEM602 4.3 13.3 1.0
C3A A:HEM602 4.3 11.3 1.0
HHD A:HEM602 4.4 11.9 1.0
HHC A:HEM602 4.4 12.6 1.0
HHA A:HEM602 4.4 15.3 1.0
HHB A:HEM602 4.4 14.2 1.0
HA3 A:GLY445 4.4 18.3 1.0
H72 A:EPE601 4.5 17.6 1.0
N A:GLY445 4.9 11.8 1.0
HE1 A:PHE436 5.0 17.7 1.0
HD12 A:ILE367 5.0 24.7 1.0
N4 A:EPE601 5.0 13.7 1.0

Reference:

B.Zhang, K.M.Lewis, A.Abril, D.R.Davydov, W.Vermerris, S.E.Sattler, C.Kang. Structure and Function of the Cytochrome P450 Monooxygenase, Cinnamate 4-Hydroxylase (C4H1) From Sorghum Bicolor. Plant Physiol. 2020.
ISSN: ESSN 1532-2548
PubMed: 32332088
DOI: 10.1104/PP.20.00406
Page generated: Wed Aug 7 13:02:46 2024

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