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Iron in PDB 1mpy: Structure of Catechol 2,3-Dioxygenase (Metapyrocatechase) From Pseudomonas Putida Mt-2

Enzymatic activity of Structure of Catechol 2,3-Dioxygenase (Metapyrocatechase) From Pseudomonas Putida Mt-2

All present enzymatic activity of Structure of Catechol 2,3-Dioxygenase (Metapyrocatechase) From Pseudomonas Putida Mt-2:
1.13.11.2;

Protein crystallography data

The structure of Structure of Catechol 2,3-Dioxygenase (Metapyrocatechase) From Pseudomonas Putida Mt-2, PDB code: 1mpy was solved by A.Kita, S.Kita, I.Fujisawa, K.Inaka, T.Ishida, K.Horiike, M.Nozaki, K.Miki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.80
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 264.000, 264.000, 59.800, 90.00, 90.00, 90.00
R / Rfree (%) 20 / 28

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Catechol 2,3-Dioxygenase (Metapyrocatechase) From Pseudomonas Putida Mt-2 (pdb code 1mpy). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Structure of Catechol 2,3-Dioxygenase (Metapyrocatechase) From Pseudomonas Putida Mt-2, PDB code: 1mpy:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1mpy

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Iron binding site 1 out of 4 in the Structure of Catechol 2,3-Dioxygenase (Metapyrocatechase) From Pseudomonas Putida Mt-2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Catechol 2,3-Dioxygenase (Metapyrocatechase) From Pseudomonas Putida Mt-2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe308

b:32.4
occ:1.00
OE1 A:GLU265 2.3 19.8 1.0
NE2 A:HIS153 2.4 18.0 1.0
NE2 A:HIS214 2.5 21.5 1.0
O A:ACN309 2.7 32.3 1.0
CD A:GLU265 3.1 11.1 1.0
CE1 A:HIS214 3.2 20.9 1.0
OE2 A:GLU265 3.3 20.6 1.0
CE1 A:HIS153 3.3 15.7 1.0
CD2 A:HIS153 3.5 15.3 1.0
OG A:SER216 3.6 23.7 1.0
CD2 A:HIS214 3.7 19.0 1.0
OH A:TYR255 3.8 21.8 1.0
C A:ACN309 4.0 30.6 1.0
NE2 A:HIS199 4.0 26.5 1.0
O A:HOH5109 4.1 9.2 1.0
CE1 A:HIS199 4.2 30.2 1.0
ND1 A:HIS214 4.4 20.2 1.0
CG A:GLU265 4.5 9.4 1.0
ND1 A:HIS153 4.5 11.7 1.0
CG A:HIS153 4.6 11.7 1.0
CG A:HIS214 4.7 16.7 1.0
CB A:SER216 4.7 17.5 1.0
NE2 A:HIS246 4.7 8.5 1.0
CE1 A:TYR255 4.8 21.1 1.0
CZ A:TYR255 4.8 20.7 1.0
C1 A:ACN309 4.9 35.2 1.0
CB A:GLU265 4.9 7.8 1.0

Iron binding site 2 out of 4 in 1mpy

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Iron binding site 2 out of 4 in the Structure of Catechol 2,3-Dioxygenase (Metapyrocatechase) From Pseudomonas Putida Mt-2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Catechol 2,3-Dioxygenase (Metapyrocatechase) From Pseudomonas Putida Mt-2 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe308

b:26.1
occ:1.00
OE1 B:GLU265 2.2 25.7 1.0
NE2 B:HIS214 2.4 16.5 1.0
O B:ACN309 2.4 37.2 1.0
NE2 B:HIS153 2.5 20.3 1.0
CD B:GLU265 2.9 20.4 1.0
CE1 B:HIS214 3.1 7.8 1.0
OE2 B:GLU265 3.1 20.9 1.0
CE1 B:HIS153 3.4 16.0 1.0
OG B:SER216 3.4 17.4 1.0
CD2 B:HIS153 3.5 16.2 1.0
CD2 B:HIS214 3.6 7.8 1.0
OH B:TYR255 3.7 10.2 1.0
C B:ACN309 3.7 38.0 1.0
NE2 B:HIS199 4.1 12.8 1.0
ND1 B:HIS214 4.3 7.8 1.0
CG B:GLU265 4.3 15.3 1.0
CE1 B:HIS199 4.5 14.7 1.0
O B:HOH5110 4.5 18.1 1.0
CG B:HIS214 4.6 7.8 1.0
ND1 B:HIS153 4.6 12.4 1.0
C1 B:ACN309 4.6 40.9 1.0
NE2 B:HIS246 4.6 13.9 1.0
CB B:GLU265 4.6 8.7 1.0
CG B:HIS153 4.7 12.4 1.0
CE1 B:TYR255 4.7 9.1 1.0
CZ B:TYR255 4.7 10.4 1.0
C2 B:ACN309 4.8 38.5 1.0
CB B:SER216 4.8 8.4 1.0

Iron binding site 3 out of 4 in 1mpy

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Iron binding site 3 out of 4 in the Structure of Catechol 2,3-Dioxygenase (Metapyrocatechase) From Pseudomonas Putida Mt-2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Structure of Catechol 2,3-Dioxygenase (Metapyrocatechase) From Pseudomonas Putida Mt-2 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe308

b:25.0
occ:1.00
OE1 C:GLU265 2.2 19.1 1.0
O C:ACN309 2.4 35.1 1.0
NE2 C:HIS214 2.5 24.3 1.0
NE2 C:HIS153 2.6 23.7 1.0
CE1 C:HIS214 2.8 25.0 1.0
CD C:GLU265 3.0 10.5 1.0
OE2 C:GLU265 3.1 14.1 1.0
CE1 C:HIS153 3.5 21.5 1.0
OG C:SER216 3.6 8.9 1.0
C C:ACN309 3.7 36.2 1.0
CD2 C:HIS153 3.7 19.1 1.0
OH C:TYR255 3.7 25.0 1.0
CD2 C:HIS214 3.8 23.3 1.0
O C:HOH5112 4.0 46.2 1.0
ND1 C:HIS214 4.1 21.9 1.0
NE2 C:HIS199 4.2 27.8 1.0
CG C:GLU265 4.4 10.2 1.0
CE1 C:TYR255 4.5 22.9 1.0
CG C:HIS214 4.6 21.2 1.0
C2 C:ACN309 4.6 34.6 1.0
CE1 C:HIS199 4.6 26.1 1.0
CZ C:TYR255 4.6 23.2 1.0
C1 C:ACN309 4.7 39.2 1.0
ND1 C:HIS153 4.7 18.9 1.0
CB C:SER216 4.7 7.8 1.0
CB C:GLU265 4.7 7.8 1.0
NE2 C:HIS246 4.8 17.4 1.0
CG C:HIS153 4.8 17.5 1.0

Iron binding site 4 out of 4 in 1mpy

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Iron binding site 4 out of 4 in the Structure of Catechol 2,3-Dioxygenase (Metapyrocatechase) From Pseudomonas Putida Mt-2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Structure of Catechol 2,3-Dioxygenase (Metapyrocatechase) From Pseudomonas Putida Mt-2 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe308

b:27.4
occ:1.00
NE2 D:HIS214 2.2 11.4 1.0
OE1 D:GLU265 2.4 15.8 1.0
NE2 D:HIS153 2.4 15.9 1.0
O D:ACN309 2.9 21.8 1.0
CE1 D:HIS214 3.1 11.6 1.0
OG D:SER216 3.3 18.6 1.0
CD2 D:HIS214 3.3 10.8 1.0
CD2 D:HIS153 3.3 13.4 1.0
CD D:GLU265 3.4 7.8 1.0
CE1 D:HIS153 3.5 12.1 1.0
OE2 D:GLU265 3.8 7.8 1.0
NE2 D:HIS199 4.0 19.1 1.0
OH D:TYR255 4.1 27.1 1.0
C D:ACN309 4.2 25.8 1.0
ND1 D:HIS214 4.3 13.9 1.0
CE1 D:HIS199 4.4 20.4 1.0
CG D:HIS214 4.4 13.0 1.0
CB D:SER216 4.5 8.1 1.0
CG D:HIS153 4.6 12.0 1.0
ND1 D:HIS153 4.6 11.8 1.0
CD1 D:LEU155 4.7 12.4 1.0
CB D:LEU155 4.7 8.2 1.0
CG D:GLU265 4.7 7.8 1.0
CE1 D:TYR255 4.9 29.0 1.0
CB D:GLU265 4.9 7.8 1.0
CZ D:TYR255 5.0 29.4 1.0

Reference:

A.Kita, S.Kita, I.Fujisawa, K.Inaka, T.Ishida, K.Horiike, M.Nozaki, K.Miki. An Archetypical Extradiol-Cleaving Catecholic Dioxygenase: the Crystal Structure of Catechol 2,3-Dioxygenase (Metapyrocatechase) From Ppseudomonas Putida Mt-2. Structure Fold.Des. V. 7 25 1999.
ISSN: ISSN 0969-2126
PubMed: 10368270
DOI: 10.1016/S0969-2126(99)80006-9
Page generated: Wed Jul 16 18:17:43 2025

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