Atomistry » Iron » PDB 4yph-4z6p » 4z6n
Atomistry »
  Iron »
    PDB 4yph-4z6p »
      4z6n »

Iron in PDB 4z6n: Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.52 Ang Resolution

Protein crystallography data

The structure of Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.52 Ang Resolution, PDB code: 4z6n 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) 45.76 / 1.52
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 110.179, 150.663, 96.067, 90.00, 90.00, 90.00
R / Rfree (%) 11.8 / 16.7

Other elements in 4z6n:

The structure of Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.52 Ang 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 H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.52 Ang Resolution (pdb code 4z6n). 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 H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.52 Ang Resolution, PDB code: 4z6n:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 4z6n

Go back to Iron Binding Sites List in 4z6n
Iron binding site 1 out of 4 in the Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.52 Ang 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 H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.52 Ang Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe401

b:18.1
occ:1.00
OE1 A:GLU267 2.1 16.4 1.0
O A:HOH726 2.2 20.2 1.0
O A:HOH744 2.2 19.2 1.0
NE2 A:HIS155 2.2 17.9 1.0
NE2 A:HIS214 2.2 17.2 1.0
O A:HOH506 2.3 21.1 1.0
CE1 A:HIS214 3.1 16.7 1.0
CE1 A:HIS155 3.1 19.6 1.0
CD A:GLU267 3.2 17.8 1.0
CD2 A:HIS155 3.2 16.4 1.0
CD2 A:HIS214 3.2 15.9 1.0
OE2 A:GLU267 3.6 17.6 1.0
OH A:TYR257 4.2 17.2 1.0
ND1 A:HIS214 4.2 18.5 1.0
ND1 A:HIS155 4.2 18.3 1.0
O A:HOH813 4.3 36.4 1.0
O A:HOH534 4.3 31.4 1.0
CG A:HIS155 4.3 19.8 1.0
CG A:HIS214 4.3 17.3 1.0
ND2 A:ASN157 4.4 19.0 1.0
CG A:GLU267 4.4 15.7 1.0
CB A:ALA216 4.6 18.3 1.0
CB A:GLU267 4.6 13.8 1.0
CB A:ASN157 4.6 18.1 1.0
CE1 A:TYR257 4.7 16.7 1.0
NE1 A:TRP192 4.8 22.9 1.0
ND2 A:ASN200 4.8 28.2 1.0
CZ A:TYR257 4.9 17.2 1.0
CE1 A:TYR269 5.0 16.7 1.0
CD1 A:TYR269 5.0 19.3 1.0

Iron binding site 2 out of 4 in 4z6n

Go back to Iron Binding Sites List in 4z6n
Iron binding site 2 out of 4 in the Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.52 Ang 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 H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.52 Ang Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe401

b:16.5
occ:1.00
OE1 B:GLU267 2.0 16.5 1.0
O B:HOH518 2.1 19.7 1.0
O B:HOH785 2.2 18.5 1.0
O B:HOH770 2.2 20.1 1.0
NE2 B:HIS155 2.2 14.3 1.0
NE2 B:HIS214 2.2 14.9 1.0
CD B:GLU267 3.1 14.6 1.0
CE1 B:HIS214 3.1 16.9 1.0
CE1 B:HIS155 3.2 14.2 1.0
CD2 B:HIS155 3.2 14.8 1.0
CD2 B:HIS214 3.3 14.7 1.0
OE2 B:GLU267 3.5 18.3 1.0
OH B:TYR257 4.2 16.7 1.0
O B:HOH826 4.2 38.0 1.0
ND1 B:HIS214 4.2 15.7 1.0
ND1 B:HIS155 4.3 14.2 1.0
O B:HOH543 4.3 35.6 1.0
CG B:HIS155 4.3 14.4 1.0
ND2 B:ASN157 4.3 16.7 1.0
CG B:HIS214 4.4 17.3 1.0
CG B:GLU267 4.4 14.7 1.0
CB B:GLU267 4.6 14.0 1.0
CB B:ALA216 4.6 15.5 1.0
CB B:ASN157 4.6 16.8 1.0
CE1 B:TYR257 4.7 15.1 1.0
NE1 B:TRP192 4.8 22.5 1.0
ND2 B:ASN200 4.8 27.8 1.0
CZ B:TYR257 4.9 15.3 1.0

Iron binding site 3 out of 4 in 4z6n

Go back to Iron Binding Sites List in 4z6n
Iron binding site 3 out of 4 in the Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.52 Ang 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 H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.52 Ang Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe401

b:15.7
occ:1.00
OE1 C:GLU267 2.0 14.6 1.0
O C:HOH708 2.2 18.3 1.0
NE2 C:HIS214 2.2 13.1 1.0
O C:HOH724 2.2 18.0 1.0
NE2 C:HIS155 2.2 15.6 1.0
O C:HOH507 2.3 20.2 1.0
CE1 C:HIS214 3.0 15.3 1.0
CD C:GLU267 3.1 14.8 1.0
CE1 C:HIS155 3.1 14.1 1.0
CD2 C:HIS214 3.3 14.3 1.0
CD2 C:HIS155 3.3 13.1 1.0
OE2 C:GLU267 3.5 17.0 1.0
O C:HOH825 4.2 25.3 0.5
OH C:TYR257 4.2 16.5 1.0
ND1 C:HIS214 4.2 13.3 1.0
ND1 C:HIS155 4.3 13.2 1.0
O C:HOH808 4.3 31.6 1.0
ND2 C:ASN157 4.3 15.5 1.0
CG C:HIS214 4.4 13.6 1.0
CG C:GLU267 4.4 13.6 1.0
CG C:HIS155 4.4 13.0 1.0
O C:HOH531 4.4 30.6 1.0
CB C:ASN157 4.6 14.8 1.0
CB C:GLU267 4.6 12.6 1.0
CE1 C:TYR257 4.6 14.7 1.0
CB C:ALA216 4.7 14.4 1.0
ND2 C:ASN200 4.7 25.9 1.0
NE1 C:TRP192 4.8 23.8 1.0
CZ C:TYR257 4.9 14.4 1.0
CG C:ASN157 4.9 13.2 1.0

Iron binding site 4 out of 4 in 4z6n

Go back to Iron Binding Sites List in 4z6n
Iron binding site 4 out of 4 in the Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.52 Ang 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 H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.52 Ang Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe401

b:15.4
occ:1.00
OE1 D:GLU267 2.1 14.2 1.0
O D:HOH512 2.1 18.8 1.0
O D:HOH758 2.2 17.6 1.0
NE2 D:HIS155 2.2 13.6 1.0
NE2 D:HIS214 2.2 12.5 1.0
O D:HOH719 2.3 18.5 1.0
CE1 D:HIS214 3.1 14.1 1.0
CE1 D:HIS155 3.1 15.3 1.0
CD D:GLU267 3.1 14.3 1.0
CD2 D:HIS155 3.2 13.6 1.0
CD2 D:HIS214 3.2 13.2 1.0
OE2 D:GLU267 3.5 14.3 1.0
OH D:TYR257 4.1 15.1 1.0
ND1 D:HIS214 4.2 14.1 1.0
ND1 D:HIS155 4.2 15.2 1.0
O D:HOH822 4.3 30.9 1.0
CG D:HIS155 4.3 12.6 1.0
CG D:HIS214 4.3 13.4 1.0
CG D:GLU267 4.4 14.6 1.0
ND2 D:ASN157 4.4 15.5 1.0
O D:HOH581 4.4 28.4 1.0
CB D:ASN157 4.6 14.1 1.0
CB D:GLU267 4.6 13.5 1.0
CB D:ALA216 4.6 12.3 1.0
CE1 D:TYR257 4.7 13.9 1.0
ND2 D:ASN200 4.7 27.8 1.0
CZ D:TYR257 4.9 14.2 1.0
NE1 D:TRP192 4.9 21.9 1.0
CG D:ASN157 5.0 15.4 1.0

Reference:

E.G.Kovaleva, M.S.Rogers, J.D.Lipscomb. Structural Basis For Substrate and Oxygen Activation in Homoprotocatechuate 2,3-Dioxygenase: Roles of Conserved Active Site Histidine 200. Biochemistry V. 54 5329 2015.
ISSN: ISSN 0006-2960
PubMed: 26267790
DOI: 10.1021/ACS.BIOCHEM.5B00709
Page generated: Mon Aug 5 17:12:27 2024

Last articles

Cl in 3RDK
Cl in 3RD7
Cl in 3RDR
Cl in 3RDB
Cl in 3RCD
Cl in 3RCG
Cl in 3RAS
Cl in 3RC7
Cl in 3RCB
Cl in 3RC9
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy