Zinc in PDB 8q58: Crystal Structure of Metal-Dependent Classii Sulfofructosephosphate Aldolase (Sfpa) From Hafnia Paralvei Hpsqia-Zn

Protein crystallography data

The structure of Crystal Structure of Metal-Dependent Classii Sulfofructosephosphate Aldolase (Sfpa) From Hafnia Paralvei Hpsqia-Zn, PDB code: 8q58 was solved by M.Sharma, G.J.Davies, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 63.01 / 1.70
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 60.332, 88.49, 126.805, 90, 90, 90
R / Rfree (%) 18.5 / 20.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Metal-Dependent Classii Sulfofructosephosphate Aldolase (Sfpa) From Hafnia Paralvei Hpsqia-Zn (pdb code 8q58). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Metal-Dependent Classii Sulfofructosephosphate Aldolase (Sfpa) From Hafnia Paralvei Hpsqia-Zn, PDB code: 8q58:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 8q58

Go back to Zinc Binding Sites List in 8q58
Zinc binding site 1 out of 2 in the Crystal Structure of Metal-Dependent Classii Sulfofructosephosphate Aldolase (Sfpa) From Hafnia Paralvei Hpsqia-Zn


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Metal-Dependent Classii Sulfofructosephosphate Aldolase (Sfpa) From Hafnia Paralvei Hpsqia-Zn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:26.0
occ:0.80
OE1 A:GLU134 1.9 27.6 1.0
NE2 A:HIS83 2.1 25.6 0.8
NE2 A:HIS180 2.2 49.0 1.0
ND1 A:HIS208 2.2 20.1 0.5
CE1 A:HIS83 2.3 25.1 0.2
O A:HOH434 2.6 32.2 1.0
CD A:GLU134 2.7 31.8 1.0
OE2 A:GLU134 2.8 32.8 1.0
NE2 A:HIS83 2.8 25.1 0.2
CD2 A:HIS208 2.9 42.8 0.5
CD2 A:HIS180 2.9 61.4 1.0
CE1 A:HIS208 3.0 23.5 0.5
CE1 A:HIS83 3.0 27.8 0.8
CD2 A:HIS83 3.2 25.8 0.8
CE1 A:HIS180 3.3 34.3 1.0
CG A:HIS208 3.3 33.8 0.5
NE2 A:HIS208 3.4 38.5 0.5
ZN A:ZN302 3.4 34.9 0.2
CG A:HIS208 3.4 21.2 0.5
ND1 A:HIS83 3.5 25.0 0.2
CB A:HIS208 3.9 29.2 0.5
CB A:HIS208 3.9 23.3 0.5
ND1 A:HIS208 3.9 38.2 0.5
CE1 A:HIS208 3.9 34.0 0.5
CG A:HIS180 4.1 63.5 1.0
CG A:GLU134 4.2 26.8 1.0
CD2 A:HIS83 4.2 25.3 0.2
O A:HOH445 4.2 32.8 1.0
ND1 A:HIS83 4.2 27.5 0.8
NE2 A:HIS208 4.2 17.5 0.5
ND1 A:HIS180 4.3 51.9 1.0
CG A:HIS83 4.3 25.2 0.8
O A:HOH515 4.3 42.5 1.0
CD2 A:HIS208 4.4 18.8 0.5
CE A:MET102 4.4 26.3 1.0
CG A:HIS83 4.4 23.9 0.2
OD2 A:ASP104 4.5 26.6 1.0
O A:HOH435 4.5 36.7 1.0
CB A:GLU134 4.8 23.4 1.0
CG A:ASP104 5.0 26.5 1.0

Zinc binding site 2 out of 2 in 8q58

Go back to Zinc Binding Sites List in 8q58
Zinc binding site 2 out of 2 in the Crystal Structure of Metal-Dependent Classii Sulfofructosephosphate Aldolase (Sfpa) From Hafnia Paralvei Hpsqia-Zn


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Metal-Dependent Classii Sulfofructosephosphate Aldolase (Sfpa) From Hafnia Paralvei Hpsqia-Zn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn302

b:34.9
occ:0.20
NE2 A:HIS83 1.8 25.1 0.2
CE1 A:HIS83 1.9 27.8 0.8
NE2 A:HIS83 2.6 25.6 0.8
CD2 A:HIS83 2.7 25.3 0.2
ND1 A:HIS208 2.8 38.2 0.5
ND1 A:HIS83 2.9 27.5 0.8
CE1 A:HIS83 3.0 25.1 0.2
CG A:HIS208 3.1 33.8 0.5
ND1 A:HIS208 3.2 20.1 0.5
CG A:HIS208 3.2 21.2 0.5
CD2 A:HIS180 3.3 61.4 1.0
CB A:HIS208 3.3 23.3 0.5
CB A:HIS208 3.3 29.2 0.5
ZN A:ZN301 3.4 26.0 0.8
O A:HOH452 3.4 42.0 1.0
O A:HOH441 3.4 49.1 1.0
O A:HOH516 3.5 56.9 1.0
CE1 A:HIS208 3.5 34.0 0.5
NE2 A:HIS180 3.6 49.0 1.0
CD2 A:HIS83 3.7 25.8 0.8
CG A:HIS83 3.8 25.2 0.8
O A:HOH513 3.9 44.8 1.0
CE1 A:HIS208 3.9 23.5 0.5
CG A:HIS83 3.9 23.9 0.2
CD2 A:HIS208 3.9 42.8 0.5
CD2 A:HIS208 3.9 18.8 0.5
ND1 A:HIS83 4.0 25.0 0.2
NE2 A:HIS208 4.1 38.5 0.5
ND2 A:ASN230 4.2 28.5 1.0
NE2 A:HIS208 4.3 17.5 0.5
CA A:HIS208 4.3 26.9 0.5
CA A:HIS208 4.3 24.7 0.5
CG A:HIS180 4.5 63.5 1.0
OD1 A:ASP82 4.5 27.7 1.0
CE1 A:HIS180 4.8 34.3 1.0
O A:HOH515 5.0 42.5 1.0
OD2 A:ASP82 5.0 33.6 1.0
N A:GLY209 5.0 34.7 1.0

Reference:

M.Sharma, A.Kaur, N.M.Soler, J.P.Lingford, R.Epa, E.D.Goddard-Borger, G.J.Davies, S.J.Williams. Defining the Molecular Architecture, Metal Dependence, and Distribution of Metal-Dependent Class II Sulfofructose-1-Phosphate Aldolases. J.Biol.Chem. 05338 2023.
ISSN: ESSN 1083-351X
PubMed: 37838169
DOI: 10.1016/J.JBC.2023.105338
Page generated: Thu Oct 31 09:57:13 2024

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