Atomistry » Iron » PDB 1phb-1q5d » 1q0c
Atomistry »
  Iron »
    PDB 1phb-1q5d »
      1q0c »

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

Go back to Iron Binding Sites List in 1q0c
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

Go back to Iron Binding Sites List in 1q0c
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

Go back to Iron Binding Sites List in 1q0c
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: Sun Dec 13 14:28:52 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy