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Iron in PDB 1kw9: Crystal Structure of 2,3-Dihydroxybiphenyl Dioxygenase (Bphc) in Complex with 2,3-Dihydroxybiphenyl at 2.0A Resolution

Enzymatic activity of Crystal Structure of 2,3-Dihydroxybiphenyl Dioxygenase (Bphc) in Complex with 2,3-Dihydroxybiphenyl at 2.0A Resolution

All present enzymatic activity of Crystal Structure of 2,3-Dihydroxybiphenyl Dioxygenase (Bphc) in Complex with 2,3-Dihydroxybiphenyl at 2.0A Resolution:
1.13.11.39;

Protein crystallography data

The structure of Crystal Structure of 2,3-Dihydroxybiphenyl Dioxygenase (Bphc) in Complex with 2,3-Dihydroxybiphenyl at 2.0A Resolution, PDB code: 1kw9 was solved by N.Sato, Y.Uragami, T.Nishizaki, Y.Takahashi, G.Sazaki, K.Sugimoto, T.Nonaka, E.Masai, M.Fukuda, T.Senda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 84.51 / 1.95
Space group I 4 2 2
Cell size a, b, c (Å), α, β, γ (°) 121.629, 121.629, 108.753, 90.00, 90.00, 90.00
R / Rfree (%) 16.1 / 18.3

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of 2,3-Dihydroxybiphenyl Dioxygenase (Bphc) in Complex with 2,3-Dihydroxybiphenyl at 2.0A Resolution (pdb code 1kw9). 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 2,3-Dihydroxybiphenyl Dioxygenase (Bphc) in Complex with 2,3-Dihydroxybiphenyl at 2.0A Resolution, PDB code: 1kw9:

Iron binding site 1 out of 1 in 1kw9

Go back to Iron Binding Sites List in 1kw9
Iron binding site 1 out of 1 in the Crystal Structure of 2,3-Dihydroxybiphenyl Dioxygenase (Bphc) in Complex with 2,3-Dihydroxybiphenyl at 2.0A Resolution


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 2,3-Dihydroxybiphenyl Dioxygenase (Bphc) in Complex with 2,3-Dihydroxybiphenyl at 2.0A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe301

b:13.1
occ:1.00
 OK2 B:BPY401 2.0 14.4 1.0
OE2 B:GLU260 2.0 14.0 1.0
O B:HOH591 2.2 34.0 1.0
OK1 B:BPY401 2.2 12.7 1.0
NE2 B:HIS145 2.2 13.1 1.0
NE2 B:HIS209 2.3 15.6 1.0
CK3 B:BPY401 2.8 14.6 1.0
CK4 B:BPY401 2.9 14.8 1.0
CE1 B:HIS145 3.0 14.7 1.0
CE1 B:HIS209 3.0 16.9 1.0
CD B:GLU260 3.2 12.4 1.0
CD2 B:HIS145 3.3 15.7 1.0
CD2 B:HIS209 3.4 16.1 1.0
OE1 B:GLU260 3.7 13.3 1.0
OH B:TYR249 3.8 14.4 1.0
O B:HOH539 4.1 24.1 1.0
NE2 B:HIS194 4.1 18.4 1.0
ND1 B:HIS145 4.2 14.5 1.0
CK2 B:BPY401 4.2 15.0 1.0
ND1 B:HIS209 4.2 14.8 1.0
CK5 B:BPY401 4.3 13.5 1.0
CG B:HIS145 4.4 14.1 1.0
CG B:GLU260 4.4 12.1 1.0
CB B:MET211 4.4 12.9 1.0
CE1 B:TYR249 4.4 11.9 1.0
CG B:HIS209 4.5 13.7 1.0
NE2 B:HIS240 4.5 15.2 1.0
CZ B:TYR249 4.5 12.6 1.0
CG2 B:VAL147 4.5 17.0 1.0
CB B:GLU260 4.5 11.7 1.0
CG B:MET211 4.7 14.4 1.0
CK7 B:BPY401 4.8 16.0 1.0
CE1 B:HIS194 4.9 17.9 1.0
CK8 B:BPY401 4.9 18.8 1.0

Reference:

N.Sato, Y.Uragami, T.Nishizaki, Y.Takahashi, G.Sazaki, K.Sugimoto, T.Nonaka, E.Masai, M.Fukuda, T.Senda. Crystal Structures of the Reaction Intermediate and Its Homologue of An Extradiol-Cleaving Catecholic Dioxygenase J.Mol.Biol. V. 321 621 2002.
ISSN: ISSN 0022-2836
PubMed: 12206778
DOI: 10.1016/S0022-2836(02)00673-3
Page generated: Sat Aug 3 09:30:30 2024

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