Iron in PDB 4iex: Unliganded Room-Temp Cysteine Dioxygenase at pH 6.2

All present enzymatic activity of Unliganded Room-Temp Cysteine Dioxygenase at pH 6.2:
1.13.11.20;

The structure of Unliganded Room-Temp Cysteine Dioxygenase at pH 6.2, PDB code: 4iex was solved by C.M.Driggers, R.B.Cooley, P.A.Karplus, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.76 / 2.15
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	57.600, 57.600, 122.400, 90.00, 90.00, 90.00
R / Rfree (%)	17.5 / 25.6

The binding sites of Iron atom in the Unliganded Room-Temp Cysteine Dioxygenase at pH 6.2 (pdb code 4iex). 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 Unliganded Room-Temp Cysteine Dioxygenase at pH 6.2, PDB code: 4iex:

Iron binding site 1 out of 1 in the Unliganded Room-Temp Cysteine Dioxygenase at pH 6.2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Unliganded Room-Temp Cysteine Dioxygenase at pH 6.2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:30.4 occ:1.00 NE2 A:HIS86 1.9 34.2 1.0 NE2 A:HIS140 2.0 29.2 1.0 O A:HOH601 2.1 31.9 1.0 NE2 A:HIS88 2.1 20.1 1.0 CE1 A:HIS86 2.7 28.3 1.0 CE1 A:HIS140 2.9 26.1 1.0 CE1 A:HIS88 3.0 37.4 1.0 CD2 A:HIS140 3.0 26.4 1.0 CD2 A:HIS86 3.0 34.8 1.0 CD2 A:HIS88 3.2 21.9 1.0 O A:HOH618 3.6 47.4 1.0 OH A:TYR157 3.9 50.8 1.0 ND1 A:HIS86 3.9 29.7 1.0 ND1 A:HIS140 4.0 20.4 1.0 CG A:HIS86 4.1 26.2 1.0 CG A:HIS140 4.1 24.2 1.0 ND1 A:HIS88 4.2 27.0 1.0 CG A:HIS88 4.3 33.5 1.0 SG A:CYS93 4.5 31.8 1.0 CG2 A:ILE133 4.8 31.9 1.0 CZ A:TYR157 4.9 34.1 1.0 O A:ASP87 5.0 32.5 1.0

C.M.Driggers, R.B.Cooley, B.Sankaran, L.L.Hirschberger, M.H.Stipanuk, P.A.Karplus. Cysteine Dioxygenase Structures From PH4 to 9: Consistent Cys-Persulfenate Formation at Intermediate pH and A Cys-Bound Enzyme at Higher pH. J.Mol.Biol. V. 425 3121 2013.
ISSN: ISSN 0022-2836
PubMed: 23747973
DOI: 10.1016/J.JMB.2013.05.028