Atomistry » Iron » PDB 3h34-3hni » 3hjq
Atomistry »
  Iron »
    PDB 3h34-3hni »
      3hjq »

Iron in PDB 3hjq: Crystal Structure of Catechol 1,2-Dioxygenase From Rhodococcus Opacus 1CP in Complex with 3-Methylcatechol

Enzymatic activity of Crystal Structure of Catechol 1,2-Dioxygenase From Rhodococcus Opacus 1CP in Complex with 3-Methylcatechol

All present enzymatic activity of Crystal Structure of Catechol 1,2-Dioxygenase From Rhodococcus Opacus 1CP in Complex with 3-Methylcatechol:
1.13.11.1;

Protein crystallography data

The structure of Crystal Structure of Catechol 1,2-Dioxygenase From Rhodococcus Opacus 1CP in Complex with 3-Methylcatechol, PDB code: 3hjq was solved by I.Matera, M.Ferraroni, 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 / 2.00
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 88.938, 37.585, 74.810, 90.00, 94.96, 90.00
R / Rfree (%) 22.7 / 27.3

Iron Binding Sites:

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

Iron binding site 1 out of 1 in 3hjq

Go back to Iron Binding Sites List in 3hjq
Iron binding site 1 out of 1 in the Crystal Structure of Catechol 1,2-Dioxygenase From Rhodococcus Opacus 1CP in Complex with 3-Methylcatechol


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 Rhodococcus Opacus 1CP in Complex with 3-Methylcatechol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe281

b:18.6
occ:1.00
 OH A:TYR162 1.8 26.8 1.0
OA1 A:MBD283 1.9 36.5 0.8
NE2 A:HIS220 2.2 13.3 1.0
NE2 A:HIS222 2.2 5.7 1.0
OA2 A:MBD283 2.3 37.4 0.8
CA1 A:MBD283 2.8 36.2 0.8
CZ A:TYR162 2.9 23.2 1.0
CE1 A:HIS220 3.0 7.9 1.0
CA2 A:MBD283 3.0 36.2 0.8
CD2 A:HIS222 3.2 10.5 1.0
CE1 A:HIS222 3.2 12.1 1.0
CD2 A:HIS220 3.3 6.8 1.0
CE1 A:TYR162 3.6 22.8 1.0
CE2 A:TYR162 3.9 22.7 1.0
O A:HOH354 3.9 14.3 1.0
NH1 A:ARG217 4.0 16.5 1.0
CA6 A:MBD283 4.2 37.5 0.8
ND1 A:HIS220 4.2 14.1 1.0
ND1 A:HIS222 4.3 10.4 1.0
CG A:HIS222 4.3 8.7 1.0
CG A:HIS220 4.3 16.1 1.0
O A:HOH299 4.5 10.6 1.0
CA3 A:MBD283 4.5 35.3 0.8
CD1 A:TYR106 4.6 27.7 1.0
CD1 A:TYR162 4.9 24.3 1.0

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 11:31:23 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy