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Iron in PDB 2ehz: Anaerobic Crystal Structure Analysis of 1,2-Dihydroxynaphthalene Dioxygenase From Pseudomonas Sp. Strain C18 Complexed with 4- Methylcatechol

Protein crystallography data

The structure of Anaerobic Crystal Structure Analysis of 1,2-Dihydroxynaphthalene Dioxygenase From Pseudomonas Sp. Strain C18 Complexed with 4- Methylcatechol, PDB code: 2ehz was solved by D.B.Neau, M.S.Kelker, C.L.Colbert, J.T.Bolin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.34 / 1.35
Space group I 4 2 2
Cell size a, b, c (Å), α, β, γ (°) 117.820, 117.820, 121.160, 90.00, 90.00, 90.00
R / Rfree (%) 16.5 / 17.8

Other elements in 2ehz:

The structure of Anaerobic Crystal Structure Analysis of 1,2-Dihydroxynaphthalene Dioxygenase From Pseudomonas Sp. Strain C18 Complexed with 4- Methylcatechol also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Anaerobic Crystal Structure Analysis of 1,2-Dihydroxynaphthalene Dioxygenase From Pseudomonas Sp. Strain C18 Complexed with 4- Methylcatechol (pdb code 2ehz). 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 Anaerobic Crystal Structure Analysis of 1,2-Dihydroxynaphthalene Dioxygenase From Pseudomonas Sp. Strain C18 Complexed with 4- Methylcatechol, PDB code: 2ehz:

Iron binding site 1 out of 1 in 2ehz

Go back to Iron Binding Sites List in 2ehz
Iron binding site 1 out of 1 in the Anaerobic Crystal Structure Analysis of 1,2-Dihydroxynaphthalene Dioxygenase From Pseudomonas Sp. Strain C18 Complexed with 4- Methylcatechol


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Anaerobic Crystal Structure Analysis of 1,2-Dihydroxynaphthalene Dioxygenase From Pseudomonas Sp. Strain C18 Complexed with 4- Methylcatechol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe399

b:8.6
occ:1.00
OE1 A:GLU266 2.0 7.6 1.0
O3 A:MCT1600 2.1 3.1 1.0
NE2 A:HIS152 2.2 6.9 1.0
NE2 A:HIS215 2.2 6.8 1.0
O4 A:MCT1600 2.2 3.5 1.0
C3 A:MCT1600 2.9 2.6 1.0
C4 A:MCT1600 3.0 3.4 1.0
CE1 A:HIS152 3.1 6.0 1.0
CD A:GLU266 3.1 7.2 1.0
CE1 A:HIS215 3.1 6.2 1.0
CD2 A:HIS215 3.2 7.7 1.0
CD2 A:HIS152 3.2 7.6 1.0
OE2 A:GLU266 3.5 8.1 1.0
OH A:TYR256 3.6 8.1 1.0
O A:HOH1606 4.0 15.1 1.0
NE2 A:HIS200 4.2 10.0 1.0
ND1 A:HIS215 4.2 7.3 1.0
ND1 A:HIS152 4.2 7.0 1.0
CB A:MET217 4.3 6.5 1.0
C2 A:MCT1600 4.3 3.0 1.0
CE2 A:TYR256 4.3 6.8 1.0
CZ A:TYR256 4.3 6.8 1.0
CG A:HIS215 4.3 7.0 1.0
NE2 A:HIS247 4.3 10.9 1.0
CG A:HIS152 4.3 6.8 1.0
C5 A:MCT1600 4.4 3.0 1.0
CG A:GLU266 4.4 6.8 1.0
CG A:MET217 4.6 6.6 1.0
CB A:GLU266 4.7 6.2 1.0
CD2 A:HIS200 4.9 11.9 1.0
CE1 A:HIS247 5.0 9.7 1.0

Reference:

D.B.Neau, M.S.Kelker, H.Maaroufi, C.L.Colbert, L.D.Eltis, J.T.Bolin. Structural Explanation For Success and Failure in the Enzymatic Ring-Cleavage of 3,4 Dihydroxybiphenyl and Related Pcb Metabolites To Be Published.
Page generated: Sun Dec 13 14:43:26 2020

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