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Iron in PDB 4z6t: Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Sulfonyl Catechol at 1.50 Ang Resolution

Protein crystallography data

The structure of Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Sulfonyl Catechol at 1.50 Ang Resolution, PDB code: 4z6t 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) 29.49 / 1.50
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 110.183, 149.939, 95.760, 90.00, 90.00, 90.00
R / Rfree (%) 11.6 / 16.2

Other elements in 4z6t:

The structure of Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Sulfonyl Catechol at 1.50 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 in Complex with 4-Sulfonyl Catechol at 1.50 Ang Resolution (pdb code 4z6t). 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 in Complex with 4-Sulfonyl Catechol at 1.50 Ang Resolution, PDB code: 4z6t:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 4z6t

Go back to Iron Binding Sites List in 4z6t
Iron binding site 1 out of 4 in the Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Sulfonyl Catechol at 1.50 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 in Complex with 4-Sulfonyl Catechol at 1.50 Ang Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe401

b:15.5
occ:1.00
O A:HOH509 2.1 18.5 1.0
OE1 A:GLU267 2.1 12.0 1.0
O A:HOH719 2.2 14.4 1.0
O A:HOH795 2.2 20.6 1.0
NE2 A:HIS214 2.2 13.3 1.0
NE2 A:HIS155 2.2 12.3 1.0
CE1 A:HIS214 3.1 12.7 1.0
CE1 A:HIS155 3.1 13.4 1.0
CD A:GLU267 3.2 14.6 1.0
CD2 A:HIS155 3.3 13.2 1.0
CD2 A:HIS214 3.3 13.6 1.0
OE2 A:GLU267 3.6 14.9 1.0
OH A:TYR257 4.1 13.5 1.0
O A:HOH506 4.2 33.2 1.0
ND1 A:HIS214 4.2 13.2 1.0
ND1 A:HIS155 4.2 12.6 1.0
ND2 A:ASN157 4.3 15.2 1.0
O A:HOH826 4.3 37.7 1.0
CG A:HIS155 4.3 13.2 1.0
CG A:HIS214 4.4 13.3 1.0
CG A:GLU267 4.5 12.7 1.0
CB A:ASN157 4.6 12.4 1.0
CB A:GLU267 4.6 12.3 1.0
CB A:ALA216 4.7 13.2 1.0
NE1 A:TRP192 4.7 15.1 1.0
CE1 A:TYR257 4.7 11.4 1.0
CZ A:TYR257 4.9 13.0 1.0
CG A:ASN157 5.0 13.6 1.0

Iron binding site 2 out of 4 in 4z6t

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Iron binding site 2 out of 4 in the Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Sulfonyl Catechol at 1.50 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 in Complex with 4-Sulfonyl Catechol at 1.50 Ang Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe401

b:14.2
occ:1.00
OE1 B:GLU267 2.1 12.1 1.0
O B:HOH510 2.1 17.8 1.0
O B:HOH724 2.1 11.2 1.0
NE2 B:HIS155 2.2 11.4 1.0
O B:HOH780 2.2 19.4 1.0
NE2 B:HIS214 2.2 11.3 1.0
CE1 B:HIS214 3.1 10.8 1.0
CD B:GLU267 3.2 12.7 1.0
CE1 B:HIS155 3.2 11.5 1.0
CD2 B:HIS155 3.2 11.9 1.0
CD2 B:HIS214 3.3 11.3 1.0
OE2 B:GLU267 3.6 14.6 1.0
OH B:TYR257 4.1 14.3 1.0
O B:HOH840 4.2 33.9 1.0
ND1 B:HIS214 4.2 12.0 1.0
ND2 B:ASN157 4.3 11.3 1.0
ND1 B:HIS155 4.3 11.2 1.0
O B:HOH535 4.3 30.6 1.0
CG B:HIS155 4.3 10.8 1.0
CG B:HIS214 4.4 12.1 1.0
CG B:GLU267 4.4 11.2 1.0
CB B:ASN157 4.6 11.1 1.0
NE1 B:TRP192 4.6 15.8 1.0
CB B:GLU267 4.6 10.6 1.0
CE1 B:TYR257 4.6 12.3 1.0
CB B:ALA216 4.7 12.0 1.0
CZ B:TYR257 4.8 12.9 1.0
ND2 B:ASN200 4.9 21.2 1.0
CG B:ASN157 5.0 10.4 1.0

Iron binding site 3 out of 4 in 4z6t

Go back to Iron Binding Sites List in 4z6t
Iron binding site 3 out of 4 in the Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Sulfonyl Catechol at 1.50 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 in Complex with 4-Sulfonyl Catechol at 1.50 Ang Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe401

b:14.4
occ:1.00
O7 C:4SX403 2.0 13.3 0.8
OE1 C:GLU267 2.0 11.8 1.0
O8 C:4SX403 2.1 9.3 0.8
NE2 C:HIS155 2.2 10.8 1.0
NE2 C:HIS214 2.2 10.4 1.0
O C:HOH647 2.6 14.4 1.0
C1 C:4SX403 2.8 13.4 0.8
C2 C:4SX403 2.9 13.9 0.8
CE1 C:HIS214 3.1 10.4 1.0
CD C:GLU267 3.1 11.1 1.0
CE1 C:HIS155 3.1 10.5 1.0
CD2 C:HIS155 3.3 9.9 1.0
CD2 C:HIS214 3.3 11.7 1.0
OE2 C:GLU267 3.5 12.4 1.0
OH C:TYR257 4.1 11.5 1.0
C6 C:4SX403 4.2 11.8 0.8
C3 C:4SX403 4.2 14.4 0.8
ND1 C:HIS214 4.2 10.5 1.0
ND1 C:HIS155 4.2 11.2 1.0
CG C:GLU267 4.3 11.4 1.0
CG C:HIS214 4.3 10.1 1.0
CG C:HIS155 4.3 10.5 1.0
CB C:GLU267 4.5 10.3 1.0
CB C:ALA216 4.5 10.4 1.0
ND2 C:ASN157 4.6 13.0 1.0
CE1 C:TYR257 4.6 10.1 1.0
CB C:ASN157 4.7 11.3 1.0
CZ C:TYR257 4.8 10.6 1.0
CD1 C:TYR269 4.8 14.1 1.0
CE1 C:TYR269 4.8 14.8 1.0
ND2 C:ASN200 4.8 18.2 1.0

Iron binding site 4 out of 4 in 4z6t

Go back to Iron Binding Sites List in 4z6t
Iron binding site 4 out of 4 in the Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Sulfonyl Catechol at 1.50 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 in Complex with 4-Sulfonyl Catechol at 1.50 Ang Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe401

b:13.6
occ:1.00
OE1 D:GLU267 2.1 11.3 1.0
O D:HOH504 2.1 15.9 1.0
O D:HOH706 2.2 12.9 1.0
O D:HOH793 2.2 20.5 1.0
NE2 D:HIS214 2.2 10.3 1.0
NE2 D:HIS155 2.2 9.6 1.0
CE1 D:HIS214 3.1 10.7 1.0
CE1 D:HIS155 3.1 10.9 1.0
CD D:GLU267 3.1 11.2 1.0
CD2 D:HIS155 3.3 10.5 1.0
CD2 D:HIS214 3.3 11.1 1.0
OE2 D:GLU267 3.6 12.3 1.0
OH D:TYR257 4.1 12.3 1.0
O D:HOH838 4.2 37.0 1.0
ND1 D:HIS214 4.2 9.9 1.0
ND1 D:HIS155 4.2 11.6 1.0
ND2 D:ASN157 4.3 10.8 1.0
O D:HOH511 4.3 34.9 1.0
CG D:HIS155 4.4 9.7 1.0
CG D:HIS214 4.4 10.5 1.0
CG D:GLU267 4.4 10.7 1.0
O D:HOH820 4.5 30.7 1.0
CB D:ASN157 4.6 10.3 1.0
CB D:GLU267 4.6 10.1 1.0
CE1 D:TYR257 4.7 9.7 1.0
CB D:ALA216 4.7 9.2 1.0
NE1 D:TRP192 4.8 13.6 1.0
CZ D:TYR257 4.9 10.8 1.0
ND2 D:ASN200 5.0 21.7 1.0
CG D:ASN157 5.0 11.2 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: Sun Dec 13 15:54:23 2020

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