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Iron in PDB 3ecj: Structure of E323L Mutant of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum at 1.65A Resolution

Enzymatic activity of Structure of E323L Mutant of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum at 1.65A Resolution

All present enzymatic activity of Structure of E323L Mutant of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum at 1.65A Resolution:
1.13.11.15;

Protein crystallography data

The structure of Structure of E323L Mutant of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum at 1.65A Resolution, PDB code: 3ecj was solved by E.G.Kovaleva, J.D.Lipscomb, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 23.46 / 1.65
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 110.711, 163.403, 101.584, 90.00, 90.00, 90.00
R / Rfree (%) 16.9 / 19.4

Other elements in 3ecj:

The structure of Structure of E323L Mutant of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum at 1.65A Resolution also contains other interesting chemical elements:

Chlorine (Cl) 4 atoms
Calcium (Ca) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Structure of E323L Mutant of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum at 1.65A Resolution (pdb code 3ecj). 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 E323L Mutant of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum at 1.65A Resolution, PDB code: 3ecj:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 3ecj

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Iron binding site 1 out of 4 in the Structure of E323L Mutant of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum at 1.65A Resolution


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of E323L Mutant of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum at 1.65A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:15.0
occ:1.00
 OE1 A:GLU267 2.1 14.5 1.0
O A:HOH802 2.1 16.6 1.0
NE2 A:HIS214 2.2 13.3 1.0
NE2 A:HIS155 2.2 15.8 1.0
O A:HOH801 2.3 15.4 1.0
O A:HOH803 2.3 19.0 1.0
CE1 A:HIS214 3.1 13.7 1.0
CE1 A:HIS155 3.1 14.1 1.0
CD A:GLU267 3.2 14.4 1.0
CD2 A:HIS214 3.2 13.6 1.0
CD2 A:HIS155 3.3 16.6 1.0
OE2 A:GLU267 3.6 15.3 1.0
NE2 A:HIS200 3.9 17.0 1.0
OH A:TYR257 4.2 14.8 1.0
ND1 A:HIS214 4.2 12.8 1.0
ND1 A:HIS155 4.2 14.8 1.0
CG A:HIS214 4.3 12.9 1.0
CG A:HIS155 4.4 16.0 1.0
ND2 A:ASN157 4.4 15.6 1.0
CG A:GLU267 4.4 11.4 1.0
O A:HOH810 4.5 19.6 1.0
CE1 A:TYR257 4.5 12.4 1.0
CB A:GLU267 4.6 12.7 1.0
CE1 A:HIS200 4.6 17.3 1.0
CB A:ALA216 4.6 14.2 1.0
CB A:ASN157 4.7 14.8 1.0
CZ A:TYR257 4.8 12.1 1.0
CD1 A:TYR269 5.0 16.4 1.0
CD2 A:HIS200 5.0 17.9 1.0

Iron binding site 2 out of 4 in 3ecj

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Iron binding site 2 out of 4 in the Structure of E323L Mutant of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum at 1.65A Resolution


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of E323L Mutant of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum at 1.65A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe500

b:14.7
occ:1.00
 OE1 B:GLU267 2.0 15.1 1.0
O B:HOH1009 2.2 14.7 1.0
O B:HOH1011 2.2 16.2 1.0
NE2 B:HIS155 2.2 16.2 1.0
NE2 B:HIS214 2.2 13.1 1.0
O B:HOH1010 2.3 17.9 1.0
CE1 B:HIS214 3.1 11.7 1.0
CD B:GLU267 3.1 14.7 1.0
CE1 B:HIS155 3.1 13.5 1.0
CD2 B:HIS155 3.2 16.0 1.0
CD2 B:HIS214 3.3 12.3 1.0
OE2 B:GLU267 3.6 14.0 1.0
NE2 B:HIS200 3.8 17.6 1.0
OH B:TYR257 4.1 13.7 1.0
ND1 B:HIS214 4.2 11.9 1.0
ND1 B:HIS155 4.3 13.2 1.0
CG B:HIS155 4.3 15.4 1.0
CG B:HIS214 4.4 12.1 1.0
CG B:GLU267 4.4 13.1 1.0
ND2 B:ASN157 4.4 14.9 1.0
CB B:GLU267 4.5 12.7 1.0
CE1 B:HIS200 4.5 17.5 1.0
CE1 B:TYR257 4.5 12.5 1.0
O B:HOH1015 4.6 19.4 1.0
CB B:ALA216 4.6 13.2 1.0
CB B:ASN157 4.7 14.2 1.0
CZ B:TYR257 4.8 13.2 1.0
CD2 B:HIS200 4.9 16.9 1.0
CD1 B:TYR269 5.0 15.8 1.0

Iron binding site 3 out of 4 in 3ecj

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Iron binding site 3 out of 4 in the Structure of E323L Mutant of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum at 1.65A Resolution


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Structure of E323L Mutant of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum at 1.65A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe500

b:14.3
occ:1.00
 OE1 C:GLU267 2.1 14.3 1.0
O C:HOH783 2.2 13.2 1.0
NE2 C:HIS214 2.2 12.7 1.0
NE2 C:HIS155 2.2 12.3 1.0
O C:HOH806 2.2 14.6 1.0
O C:HOH807 2.3 15.9 1.0
CE1 C:HIS214 3.1 11.4 1.0
CE1 C:HIS155 3.1 13.5 1.0
CD C:GLU267 3.2 11.4 1.0
CD2 C:HIS214 3.2 13.7 1.0
CD2 C:HIS155 3.3 13.0 1.0
OE2 C:GLU267 3.6 14.1 1.0
NE2 C:HIS200 3.9 14.3 1.0
OH C:TYR257 4.2 14.6 1.0
ND1 C:HIS214 4.2 11.2 1.0
ND1 C:HIS155 4.2 11.9 1.0
ND2 C:ASN157 4.3 15.9 1.0
CG C:HIS214 4.3 13.4 1.0
CG C:HIS155 4.4 11.9 1.0
O C:HOH808 4.4 23.4 1.0
CG C:GLU267 4.4 11.0 1.0
CE1 C:TYR257 4.5 10.3 1.0
CE1 C:HIS200 4.6 16.1 1.0
CB C:GLU267 4.6 11.6 1.0
CB C:ALA216 4.6 11.6 1.0
CB C:ASN157 4.7 12.1 1.0
CZ C:TYR257 4.8 11.6 1.0
CD1 C:TYR269 4.9 17.1 1.0
CG C:ASN157 5.0 14.9 1.0

Iron binding site 4 out of 4 in 3ecj

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Iron binding site 4 out of 4 in the Structure of E323L Mutant of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum at 1.65A Resolution


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Structure of E323L Mutant of Homoprotocatechuate 2,3-Dioxygenase From Brevibacterium Fuscum at 1.65A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe500

b:11.9
occ:1.00
 OE1 D:GLU267 2.0 10.9 1.0
O D:HOH799 2.1 13.5 1.0
NE2 D:HIS155 2.2 9.9 1.0
O D:HOH832 2.2 13.6 1.0
NE2 D:HIS214 2.3 12.4 1.0
O D:HOH833 2.3 11.8 1.0
CD D:GLU267 3.1 10.1 1.0
CE1 D:HIS155 3.1 10.4 1.0
CE1 D:HIS214 3.2 10.3 1.0
CD2 D:HIS155 3.2 12.5 1.0
CD2 D:HIS214 3.2 10.2 1.0
OE2 D:GLU267 3.6 13.6 1.0
NE2 D:HIS200 3.9 13.3 1.0
OH D:TYR257 4.1 11.5 1.0
ND1 D:HIS155 4.3 10.0 1.0
ND1 D:HIS214 4.3 9.4 1.0
CG D:HIS155 4.4 10.1 1.0
CG D:HIS214 4.4 9.2 1.0
ND2 D:ASN157 4.4 12.2 1.0
CG D:GLU267 4.4 9.5 1.0
O D:HOH835 4.5 18.9 1.0
CE1 D:HIS200 4.5 11.7 1.0
CB D:GLU267 4.6 9.2 1.0
CE1 D:TYR257 4.6 10.3 1.0
CB D:ALA216 4.6 9.8 1.0
CB D:ASN157 4.6 9.9 1.0
CZ D:TYR257 4.8 8.6 1.0
CD1 D:TYR269 4.9 14.6 1.0
CD2 D:HIS200 5.0 13.8 1.0

Reference:

E.G.Kovaleva, J.D.Lipscomb. Intermediate in the O-O Bond Cleavage Reaction of An Extradiol Dioxygenase. Biochemistry V. 47 11168 2008.
ISSN: ISSN 0006-2960
PubMed: 18826259
DOI: 10.1021/BI801459Q
Page generated: Sun Dec 13 15:04:49 2020

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