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Iron in PDB 3hgi: Crystal Structure of Catechol 1,2-Dioxygenase From the Gram-Positive Rhodococcus Opacus 1CP

Enzymatic activity of Crystal Structure of Catechol 1,2-Dioxygenase From the Gram-Positive Rhodococcus Opacus 1CP

All present enzymatic activity of Crystal Structure of Catechol 1,2-Dioxygenase From the Gram-Positive Rhodococcus Opacus 1CP:
1.13.11.1;

Protein crystallography data

The structure of Crystal Structure of Catechol 1,2-Dioxygenase From the Gram-Positive Rhodococcus Opacus 1CP, PDB code: 3hgi was solved by M.Ferraroni, I.Matera, F.Briganti, A.Scozzafava, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.94
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 89.794, 38.118, 76.065, 90.00, 94.21, 90.00
R / Rfree (%) 19.9 / 27.8

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Catechol 1,2-Dioxygenase From the Gram-Positive Rhodococcus Opacus 1CP (pdb code 3hgi). 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 Catechol 1,2-Dioxygenase From the Gram-Positive Rhodococcus Opacus 1CP, PDB code: 3hgi:

Iron binding site 1 out of 1 in 3hgi

Go back to Iron Binding Sites List in 3hgi
Iron binding site 1 out of 1 in the Crystal Structure of Catechol 1,2-Dioxygenase From the Gram-Positive Rhodococcus Opacus 1CP


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 Catechol 1,2-Dioxygenase From the Gram-Positive Rhodococcus Opacus 1CP within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe281

b:21.8
occ:1.00
O1 A:BEZ284 1.7 28.6 1.0
OH A:TYR162 1.8 28.9 1.0
NE2 A:HIS222 2.2 10.4 1.0
NE2 A:HIS220 2.2 17.2 1.0
OH A:TYR196 2.3 23.2 1.0
C A:BEZ284 2.5 26.6 1.0
O2 A:BEZ284 2.5 26.7 1.0
O2 A:CO3282 2.7 11.5 0.5
CZ A:TYR162 2.9 23.7 1.0
CE1 A:HIS220 3.0 19.9 1.0
CD2 A:HIS222 3.1 9.8 1.0
CE1 A:HIS222 3.2 14.3 1.0
CD2 A:HIS220 3.3 16.9 1.0
CZ A:TYR196 3.5 27.6 1.0
CE1 A:TYR162 3.6 25.3 1.0
CE2 A:TYR162 3.8 25.9 1.0
C A:CO3282 3.8 11.1 0.5
CE1 A:TYR196 3.9 26.9 1.0
C1 A:BEZ284 4.0 27.4 1.0
O3 A:CO3282 4.1 13.1 0.5
NH1 A:ARG217 4.2 19.6 1.0
ND1 A:HIS220 4.2 19.7 1.0
CG A:HIS222 4.2 16.3 1.0
ND1 A:HIS222 4.3 15.5 1.0
CG A:HIS220 4.4 20.8 1.0
O A:HOH303 4.5 17.7 1.0
C2 A:BEZ284 4.6 27.3 1.0
CE2 A:TYR196 4.7 26.8 1.0
CD1 A:TYR162 4.9 22.2 1.0
CD1 A:TYR106 4.9 31.3 1.0
O1 A:CO3282 5.0 16.5 0.5

Reference:

I.Matera, M.Ferraroni, M.Kolomytseva, L.Golovleva, A.Scozzafava, F.Briganti. Catechol 1,2-Dioxygenase From the Gram-Positive Rhodococcus Opacus 1CP: Quantitative Structure/Activity Relationship and the Crystal Structures of Native Enzyme and Catechols Adducts. J.Struct.Biol. V. 170 548 2010.
ISSN: ISSN 1047-8477
PubMed: 20040374
DOI: 10.1016/J.JSB.2009.12.023
Page generated: Sun Aug 4 11:29:52 2024

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