Atomistry » Iron » PDB 3ebd-3esf » 3ecj
Atomistry »
  Iron »
    PDB 3ebd-3esf »
      3ecj »

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

Go back to Iron Binding Sites List in 3ecj
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

Go back to Iron Binding Sites List in 3ecj
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

Go back to Iron Binding Sites List in 3ecj
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

Go back to Iron Binding Sites List in 3ecj
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 Aug 4 09:42:04 2024

Last articles

Ca in 2OKX
Ca in 2OMY
Ca in 2OMV
Ca in 2OMX
Ca in 2OMU
Ca in 2OMT
Ca in 2OLG
Ca in 2OKS
Ca in 2OG9
Ca in 2OGY
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy