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Iron in PDB 1kmy: Crystal Structure of 2,3-Dihydroxybiphenyl 1,2-Dioxygenase Complexed with 2,3-Dihydroxybiphenyl Under Anaerobic Condition

Enzymatic activity of Crystal Structure of 2,3-Dihydroxybiphenyl 1,2-Dioxygenase Complexed with 2,3-Dihydroxybiphenyl Under Anaerobic Condition

All present enzymatic activity of Crystal Structure of 2,3-Dihydroxybiphenyl 1,2-Dioxygenase Complexed with 2,3-Dihydroxybiphenyl Under Anaerobic Condition:
1.13.11.39;

Protein crystallography data

The structure of Crystal Structure of 2,3-Dihydroxybiphenyl 1,2-Dioxygenase Complexed with 2,3-Dihydroxybiphenyl Under Anaerobic Condition, PDB code: 1kmy was solved by S.Han, J.T.Bolin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 7.00 / 2.00
Space group I 4 2 2
Cell size a, b, c (Å), α, β, γ (°) 123.300, 123.300, 110.900, 90.00, 90.00, 90.00
R / Rfree (%) 16.3 / 19.6

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of 2,3-Dihydroxybiphenyl 1,2-Dioxygenase Complexed with 2,3-Dihydroxybiphenyl Under Anaerobic Condition (pdb code 1kmy). 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 1,2-Dioxygenase Complexed with 2,3-Dihydroxybiphenyl Under Anaerobic Condition, PDB code: 1kmy:

Iron binding site 1 out of 1 in 1kmy

Go back to Iron Binding Sites List in 1kmy
Iron binding site 1 out of 1 in the Crystal Structure of 2,3-Dihydroxybiphenyl 1,2-Dioxygenase Complexed with 2,3-Dihydroxybiphenyl Under Anaerobic Condition


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 1,2-Dioxygenase Complexed with 2,3-Dihydroxybiphenyl Under Anaerobic Condition within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:17.7
occ:1.00
 OK2 A:BPY300 2.0 20.8 1.0
OE2 A:GLU260 2.0 11.2 1.0
NE2 A:HIS146 2.2 14.7 1.0
NE2 A:HIS210 2.3 15.6 1.0
OK1 A:BPY300 2.4 22.6 1.0
O A:HOH9003 2.4 23.1 1.0
CK3 A:BPY300 2.9 24.3 1.0
CE1 A:HIS146 3.0 12.5 1.0
CK4 A:BPY300 3.0 23.3 1.0
CE1 A:HIS210 3.0 16.2 1.0
CD A:GLU260 3.2 10.6 1.0
CD2 A:HIS146 3.4 16.4 1.0
CD2 A:HIS210 3.4 14.6 1.0
OE1 A:GLU260 3.7 13.1 1.0
OH A:TYR250 3.9 14.8 1.0
O A:HOH9002 4.0 25.2 1.0
NE2 A:HIS195 4.1 16.0 1.0
CK2 A:BPY300 4.2 25.1 1.0
ND1 A:HIS146 4.2 13.1 1.0
ND1 A:HIS210 4.3 17.2 1.0
CG A:GLU260 4.4 9.3 1.0
CK5 A:BPY300 4.4 19.7 1.0
CG A:HIS146 4.4 14.3 1.0
CB A:MET212 4.4 12.4 0.5
CB A:GLU260 4.4 10.8 1.0
CB A:MET212 4.5 10.3 0.5
CG A:HIS210 4.5 16.1 1.0
NE2 A:HIS241 4.6 17.6 1.0
CZ A:TYR250 4.6 14.1 1.0
CG A:MET212 4.6 14.1 0.5
CE2 A:TYR250 4.6 14.7 1.0
CE1 A:HIS195 4.7 15.2 1.0
CG2 A:VAL148 4.7 15.9 1.0
CK7 A:BPY300 4.7 27.6 1.0
CG A:MET212 4.8 10.2 0.5

Reference:

F.H.Vaillancourt, S.Han, P.D.Fortin, J.T.Bolin, L.D.Eltis. Molecular Basis For the Stabilization and Inhibition of 2, 3-Dihydroxybiphenyl 1,2-Dioxygenase By T-Butanol. J.Biol.Chem. V. 273 34887 1998.
ISSN: ISSN 0021-9258
PubMed: 9857017
DOI: 10.1074/JBC.273.52.34887
Page generated: Sat Aug 3 09:16:26 2024

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