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Iron in PDB 4tt5: Crystal Structure of CYP119 From Sulfolobus Acidocaldarius, Complexed with 4-(4-Bromophenyl)-1H Imidazole

Enzymatic activity of Crystal Structure of CYP119 From Sulfolobus Acidocaldarius, Complexed with 4-(4-Bromophenyl)-1H Imidazole

All present enzymatic activity of Crystal Structure of CYP119 From Sulfolobus Acidocaldarius, Complexed with 4-(4-Bromophenyl)-1H Imidazole:
1.11.1.7;

Protein crystallography data

The structure of Crystal Structure of CYP119 From Sulfolobus Acidocaldarius, Complexed with 4-(4-Bromophenyl)-1H Imidazole, PDB code: 4tt5 was solved by Y.Madrona, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.86 / 2.18
Space group P 63 2 2
Cell size a, b, c (Å), α, β, γ (°) 165.340, 165.340, 76.810, 90.00, 90.00, 120.00
R / Rfree (%) 18.2 / 22.1

Other elements in 4tt5:

The structure of Crystal Structure of CYP119 From Sulfolobus Acidocaldarius, Complexed with 4-(4-Bromophenyl)-1H Imidazole also contains other interesting chemical elements:

Bromine (Br) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of CYP119 From Sulfolobus Acidocaldarius, Complexed with 4-(4-Bromophenyl)-1H Imidazole (pdb code 4tt5). 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 CYP119 From Sulfolobus Acidocaldarius, Complexed with 4-(4-Bromophenyl)-1H Imidazole, PDB code: 4tt5:

Iron binding site 1 out of 1 in 4tt5

Go back to Iron Binding Sites List in 4tt5
Iron binding site 1 out of 1 in the Crystal Structure of CYP119 From Sulfolobus Acidocaldarius, Complexed with 4-(4-Bromophenyl)-1H Imidazole


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 CYP119 From Sulfolobus Acidocaldarius, Complexed with 4-(4-Bromophenyl)-1H Imidazole within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe401

b:31.8
occ:1.00
 FE A:HEM401 0.0 31.8 1.0
N3 A:36Y402 2.0 33.4 1.0
NC A:HEM401 2.0 29.6 1.0
NA A:HEM401 2.0 27.0 1.0
ND A:HEM401 2.1 28.2 1.0
NB A:HEM401 2.1 31.7 1.0
SG A:CYS317 2.3 34.1 1.0
C2 A:36Y402 2.8 27.9 1.0
C4C A:HEM401 3.0 32.1 1.0
C1A A:HEM401 3.0 31.6 1.0
C1C A:HEM401 3.0 34.7 1.0
C4A A:HEM401 3.1 35.0 1.0
C4B A:HEM401 3.1 30.7 1.0
C1D A:HEM401 3.1 29.2 1.0
C4D A:HEM401 3.1 31.9 1.0
C4 A:36Y402 3.1 31.1 1.0
C1B A:HEM401 3.1 31.8 1.0
CB A:CYS317 3.4 33.3 1.0
CHC A:HEM401 3.4 28.9 1.0
CHA A:HEM401 3.4 31.8 1.0
CHD A:HEM401 3.4 30.6 1.0
CHB A:HEM401 3.5 31.5 1.0
N1 A:36Y402 4.0 35.0 1.0
C5 A:36Y402 4.2 33.1 1.0
CA A:CYS317 4.2 31.3 1.0
C3C A:HEM401 4.2 29.9 1.0
C3A A:HEM401 4.3 34.7 1.0
C2A A:HEM401 4.3 31.3 1.0
C2C A:HEM401 4.3 34.9 1.0
C3B A:HEM401 4.3 32.3 1.0
C2D A:HEM401 4.3 31.3 1.0
C2B A:HEM401 4.3 30.9 1.0
C3D A:HEM401 4.3 29.4 1.0
N A:GLY319 4.6 30.3 1.0
C A:CYS317 4.8 33.8 1.0
N A:LEU318 4.9 31.3 1.0

Reference:

D.Basudhar, Y.Madrona, P.Ortiz De Montellano. uc(Nmr) and X-Ray Analysis of CYP119 Ligand-Dependent Conformational Changes To Be Published.
Page generated: Sun Dec 13 15:47:38 2020

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