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Iron in PDB 1q0c: Anerobic Substrate Complex of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum. (Complex with 3,4-Dihydroxyphenylacetate)

Enzymatic activity of Anerobic Substrate Complex of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum. (Complex with 3,4-Dihydroxyphenylacetate)

All present enzymatic activity of Anerobic Substrate Complex of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum. (Complex with 3,4-Dihydroxyphenylacetate):
1.13.11.15;

Protein crystallography data

The structure of Anerobic Substrate Complex of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum. (Complex with 3,4-Dihydroxyphenylacetate), PDB code: 1q0c was solved by M.W.Vetting, L.P.Wackett, L.Que, J.D.Lipscomb, D.H.Ohlendorf, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.10
Space group I 41
Cell size a, b, c (Å), α, β, γ (°) 157.000, 157.000, 122.300, 90.00, 90.00, 90.00
R / Rfree (%) 17 / 23.4

Iron Binding Sites:

The binding sites of Iron atom in the Anerobic Substrate Complex of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum. (Complex with 3,4-Dihydroxyphenylacetate) (pdb code 1q0c). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Anerobic Substrate Complex of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum. (Complex with 3,4-Dihydroxyphenylacetate), PDB code: 1q0c:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1q0c

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Iron binding site 1 out of 4 in the Anerobic Substrate Complex of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum. (Complex with 3,4-Dihydroxyphenylacetate)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Anerobic Substrate Complex of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum. (Complex with 3,4-Dihydroxyphenylacetate) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:43.8
occ:1.00
 O3 A:DHY999 2.0 50.6 1.0
OE1 A:GLU267 2.1 35.0 1.0
NE2 A:HIS155 2.2 31.3 1.0
NE2 A:HIS214 2.3 33.5 1.0
O4 A:DHY999 2.3 45.7 1.0
C3 A:DHY999 3.1 46.5 1.0
CD A:GLU267 3.1 34.3 1.0
CE1 A:HIS155 3.1 32.2 1.0
C4 A:DHY999 3.2 47.3 1.0
CE1 A:HIS214 3.2 33.1 1.0
CD2 A:HIS214 3.2 33.7 1.0
CD2 A:HIS155 3.3 30.0 1.0
OE2 A:GLU267 3.6 34.0 1.0
OH A:TYR257 3.9 31.6 1.0
NE2 A:HIS200 4.0 33.5 1.0
ND1 A:HIS214 4.3 35.4 1.0
ND1 A:HIS155 4.3 29.2 1.0
CG A:HIS214 4.3 36.1 1.0
CG A:GLU267 4.3 30.8 1.0
CG A:HIS155 4.4 31.4 1.0
C2 A:DHY999 4.4 46.8 1.0
CB A:ALA216 4.4 28.5 1.0
CB A:GLU267 4.4 28.8 1.0
ND2 A:ASN157 4.5 46.3 1.0
CE1 A:TYR257 4.5 28.5 1.0
C5 A:DHY999 4.6 46.4 1.0
CZ A:TYR257 4.6 28.6 1.0
CE1 A:HIS200 4.7 35.7 1.0
CB A:ASN157 4.7 41.9 1.0
CD2 A:TYR269 5.0 41.0 1.0
NE2 A:HIS248 5.0 41.8 1.0

Iron binding site 2 out of 4 in 1q0c

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Iron binding site 2 out of 4 in the Anerobic Substrate Complex of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum. (Complex with 3,4-Dihydroxyphenylacetate)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Anerobic Substrate Complex of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum. (Complex with 3,4-Dihydroxyphenylacetate) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe500

b:42.5
occ:1.00
 OE1 B:GLU267 1.9 36.7 1.0
O3 B:DHY999 2.0 41.5 1.0
NE2 B:HIS214 2.1 27.1 1.0
NE2 B:HIS155 2.3 32.0 1.0
O4 B:DHY999 2.4 43.6 1.0
CE1 B:HIS214 3.0 29.9 1.0
CD B:GLU267 3.1 32.8 1.0
C3 B:DHY999 3.1 41.5 1.0
CE1 B:HIS155 3.2 33.7 1.0
CD2 B:HIS214 3.2 30.2 1.0
C4 B:DHY999 3.3 43.4 1.0
CD2 B:HIS155 3.3 33.5 1.0
OE2 B:GLU267 3.5 35.5 1.0
NE2 B:HIS200 3.9 33.5 1.0
OH B:TYR257 4.0 33.2 1.0
ND1 B:HIS214 4.1 27.8 1.0
CG B:HIS214 4.3 31.1 1.0
CG B:GLU267 4.3 31.8 1.0
ND1 B:HIS155 4.3 32.1 1.0
C2 B:DHY999 4.4 43.1 1.0
CB B:GLU267 4.4 30.4 1.0
CG B:HIS155 4.5 33.9 1.0
ND2 B:ASN157 4.5 38.5 1.0
CE1 B:TYR257 4.5 31.9 1.0
CB B:ALA216 4.5 32.0 1.0
CE1 B:HIS200 4.6 32.3 1.0
CZ B:TYR257 4.7 31.8 1.0
CB B:ASN157 4.7 38.5 1.0
C5 B:DHY999 4.7 40.4 1.0
NE2 B:HIS248 4.9 37.9 1.0
CD2 B:HIS200 5.0 36.0 1.0

Iron binding site 3 out of 4 in 1q0c

Go back to Iron Binding Sites List in 1q0c
Iron binding site 3 out of 4 in the Anerobic Substrate Complex of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum. (Complex with 3,4-Dihydroxyphenylacetate)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Anerobic Substrate Complex of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum. (Complex with 3,4-Dihydroxyphenylacetate) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe500

b:34.2
occ:1.00
 OE1 C:GLU267 1.9 28.3 1.0
O3 C:DHY999 2.1 44.3 1.0
NE2 C:HIS155 2.2 22.5 1.0
NE2 C:HIS214 2.2 25.9 1.0
O4 C:DHY999 2.3 47.6 1.0
CE1 C:HIS155 3.1 24.2 1.0
C3 C:DHY999 3.1 45.5 1.0
CD C:GLU267 3.1 28.1 1.0
CD2 C:HIS214 3.2 27.9 1.0
CD2 C:HIS155 3.2 18.3 1.0
CE1 C:HIS214 3.2 29.8 1.0
C4 C:DHY999 3.2 46.6 1.0
OE2 C:GLU267 3.7 28.3 1.0
OH C:TYR257 3.9 30.0 1.0
NE2 C:HIS200 4.0 27.3 1.0
ND2 C:ASN157 4.2 35.9 1.0
ND1 C:HIS155 4.2 20.4 1.0
CG C:HIS155 4.3 22.2 1.0
ND1 C:HIS214 4.3 27.2 1.0
CG C:HIS214 4.3 29.3 1.0
CG C:GLU267 4.4 28.3 1.0
CB C:ALA216 4.4 27.4 1.0
C2 C:DHY999 4.5 44.8 1.0
CE1 C:TYR257 4.5 27.6 1.0
CB C:GLU267 4.5 27.8 1.0
CB C:ASN157 4.6 31.0 1.0
C5 C:DHY999 4.6 45.6 1.0
CE1 C:HIS200 4.6 27.5 1.0
CZ C:TYR257 4.6 28.4 1.0
CG C:ASN157 4.9 34.8 1.0

Iron binding site 4 out of 4 in 1q0c

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Iron binding site 4 out of 4 in the Anerobic Substrate Complex of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum. (Complex with 3,4-Dihydroxyphenylacetate)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Anerobic Substrate Complex of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum. (Complex with 3,4-Dihydroxyphenylacetate) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe500

b:37.6
occ:1.00
 O3 D:DHY999 2.0 44.7 1.0
OE1 D:GLU267 2.0 31.1 1.0
O4 D:DHY999 2.2 46.6 1.0
NE2 D:HIS155 2.2 24.4 1.0
NE2 D:HIS214 2.2 27.6 1.0
C3 D:DHY999 3.0 43.3 1.0
CD D:GLU267 3.0 30.3 1.0
CE1 D:HIS155 3.0 25.4 1.0
C4 D:DHY999 3.1 44.9 1.0
CE1 D:HIS214 3.2 28.6 1.0
CD2 D:HIS214 3.2 26.9 1.0
CD2 D:HIS155 3.2 23.9 1.0
OE2 D:GLU267 3.5 33.3 1.0
OH D:TYR257 3.9 29.6 1.0
NE2 D:HIS200 3.9 27.4 1.0
ND1 D:HIS155 4.2 25.3 1.0
ND1 D:HIS214 4.3 26.8 1.0
CG D:GLU267 4.3 28.8 1.0
CG D:HIS214 4.3 28.4 1.0
CG D:HIS155 4.3 25.8 1.0
C2 D:DHY999 4.3 44.0 1.0
CE1 D:TYR257 4.4 25.3 1.0
CB D:GLU267 4.4 27.5 1.0
ND2 D:ASN157 4.4 32.7 1.0
C5 D:DHY999 4.4 42.5 1.0
CB D:ALA216 4.5 26.5 1.0
CB D:ASN157 4.6 31.6 1.0
CZ D:TYR257 4.6 27.3 1.0
CE1 D:HIS200 4.7 25.8 1.0
CD2 D:HIS200 5.0 23.7 1.0
CD2 D:TYR269 5.0 42.8 1.0

Reference:

M.W.Vetting, L.P.Wackett, L.Que, J.D.Lipscomb, D.H.Ohlendorf. Crystallographic Comparison of Manganese- and Iron-Dependent Homoprotocatechuate 2,3-Dioxygenases. J.Bacteriol. V. 186 1945 2004.
ISSN: ISSN 0021-9193
PubMed: 15028678
DOI: 10.1128/JB.186.7.1945-1958.2004
Page generated: Sat Aug 3 13:14:53 2024

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