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Iron in PDB 1gp6: Anthocyanidin Synthase From Arabidopsis Thaliana Complexed with Trans-Dihydroquercetin (with 30 Min Exposure to O2)

Enzymatic activity of Anthocyanidin Synthase From Arabidopsis Thaliana Complexed with Trans-Dihydroquercetin (with 30 Min Exposure to O2)

All present enzymatic activity of Anthocyanidin Synthase From Arabidopsis Thaliana Complexed with Trans-Dihydroquercetin (with 30 Min Exposure to O2):
1.14.11.19;

Protein crystallography data

The structure of Anthocyanidin Synthase From Arabidopsis Thaliana Complexed with Trans-Dihydroquercetin (with 30 Min Exposure to O2), PDB code: 1gp6 was solved by R.C.Wilmouth, J.J.Turnbull, R.W.D.Welford, I.J.Clifton, A.G.Prescott, C.J.Schofield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.0 / 1.75
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 61.258, 72.385, 87.054, 90.00, 90.00, 90.00
R / Rfree (%) 19.4 / 22.2

Iron Binding Sites:

The binding sites of Iron atom in the Anthocyanidin Synthase From Arabidopsis Thaliana Complexed with Trans-Dihydroquercetin (with 30 Min Exposure to O2) (pdb code 1gp6). 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 Anthocyanidin Synthase From Arabidopsis Thaliana Complexed with Trans-Dihydroquercetin (with 30 Min Exposure to O2), PDB code: 1gp6:

Iron binding site 1 out of 1 in 1gp6

Go back to Iron Binding Sites List in 1gp6
Iron binding site 1 out of 1 in the Anthocyanidin Synthase From Arabidopsis Thaliana Complexed with Trans-Dihydroquercetin (with 30 Min Exposure to O2)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Anthocyanidin Synthase From Arabidopsis Thaliana Complexed with Trans-Dihydroquercetin (with 30 Min Exposure to O2) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe390

b:13.6
occ:1.00
 OD1 A:ASP234 2.1 10.4 1.0
O2 A:SIN370 2.2 18.8 1.0
NE2 A:HIS288 2.2 12.9 1.0
O A:HOH2267 2.2 11.9 1.0
O A:HOH2349 2.3 14.9 1.0
NE2 A:HIS232 2.3 12.9 1.0
C1 A:SIN370 3.1 22.6 1.0
CG A:ASP234 3.1 12.3 1.0
CE1 A:HIS232 3.1 12.5 1.0
CE1 A:HIS288 3.2 14.7 1.0
CD2 A:HIS288 3.2 13.3 1.0
O1 A:SIN370 3.4 26.0 1.0
CD2 A:HIS232 3.4 13.1 1.0
OD2 A:ASP234 3.4 14.6 1.0
O A:HOH2290 3.9 16.4 1.0
O13 A:QUE380 4.1 16.2 1.0
ND1 A:HIS288 4.3 12.8 1.0
CG A:HIS288 4.3 12.5 1.0
ND1 A:HIS232 4.3 11.4 1.0
C2 A:SIN370 4.5 24.6 1.0
CG A:HIS232 4.5 13.9 1.0
CB A:ASP234 4.5 12.3 1.0
O30 A:QUE380 4.6 18.6 1.0
CE2 A:PHE304 4.8 13.5 1.0
CA A:ASP234 4.8 13.0 1.0
N A:ASP234 4.9 11.1 1.0
C3 A:SIN370 4.9 24.4 1.0

Reference:

R.C.Wilmouth, J.J.Turnbull, R.W.D.Welford, I.J.Clifton, A.G.Prescott, C.J.Schofield. Structure and Mechanism of Anthocyanidin Synthase From Arabidopsis Thaliana. Structure V. 10 93 2002.
ISSN: ISSN 0969-2126
PubMed: 11796114
DOI: 10.1016/S0969-2126(01)00695-5
Page generated: Wed Jul 16 15:02:55 2025

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