Zinc in PDB 7qta: S1 Nuclease From Aspergillus Oryzae in Complex with Uridine

Enzymatic activity of S1 Nuclease From Aspergillus Oryzae in Complex with Uridine

All present enzymatic activity of S1 Nuclease From Aspergillus Oryzae in Complex with Uridine:
3.1.30.1;

Protein crystallography data

The structure of S1 Nuclease From Aspergillus Oryzae in Complex with Uridine, PDB code: 7qta was solved by K.Adamkova, T.Koval, P.Kolenko, L.H.Oestergaard, J.Dohnalek, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.20 / 1.06
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 43.04, 48.186, 65.232, 107.18, 90.11, 105.62
R / Rfree (%) 11.8 / 14.7

Other elements in 7qta:

The structure of S1 Nuclease From Aspergillus Oryzae in Complex with Uridine also contains other interesting chemical elements:

Sodium (Na) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the S1 Nuclease From Aspergillus Oryzae in Complex with Uridine (pdb code 7qta). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the S1 Nuclease From Aspergillus Oryzae in Complex with Uridine, PDB code: 7qta:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6;

Zinc binding site 1 out of 6 in 7qta

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Zinc binding site 1 out of 6 in the S1 Nuclease From Aspergillus Oryzae in Complex with Uridine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of S1 Nuclease From Aspergillus Oryzae in Complex with Uridine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:8.3
occ:1.00
O2 A:PO4406 1.9 12.3 0.2
O A:HOH670 2.0 6.6 0.5
NE2 A:HIS26 2.0 7.8 1.0
O4 A:PO4406 2.0 12.2 0.3
N A:TRP21 2.1 8.8 1.0
OD1 A:ASP139 2.1 8.1 1.0
O A:TRP21 2.2 8.6 1.0
C A:TRP21 2.9 8.0 1.0
CA A:TRP21 2.9 9.2 1.0
CE1 A:HIS26 3.0 7.7 1.0
CD2 A:HIS26 3.0 8.1 1.0
P A:PO4406 3.1 11.3 0.2
CG A:ASP139 3.1 7.4 1.0
P A:PO4406 3.1 12.0 0.3
O2 A:PO4406 3.3 13.6 0.3
ZN A:ZN402 3.3 9.0 1.0
O A:HOH519 3.4 13.6 0.5
O1 A:PO4406 3.5 12.5 0.2
OD2 A:ASP139 3.5 8.2 1.0
O4 A:PO4406 3.5 9.5 0.2
CB A:TRP21 3.6 9.1 1.0
OD2 A:ASP65 3.9 12.5 1.0
NE2 A:HIS135 3.9 8.4 1.0
O1 A:PO4406 3.9 11.9 0.3
CE1 A:HIS135 4.1 8.3 1.0
CE1 A:HIS145 4.1 9.3 1.0
ND1 A:HIS26 4.1 7.9 1.0
CG A:HIS26 4.1 7.9 1.0
N A:GLY22 4.2 8.9 1.0
NE2 A:HIS145 4.2 9.7 1.0
O3 A:PO4406 4.3 8.2 0.2
CG A:TRP21 4.3 9.0 1.0
O3 A:PO4406 4.4 11.4 0.3
CB A:ASP139 4.4 7.3 1.0
CD1 A:TRP21 4.4 9.0 1.0
OD1 A:ASP172 4.6 9.6 1.0
ZN A:ZN403 4.6 10.9 1.0
CA A:ASP139 4.7 7.6 1.0
CG A:ASP65 4.8 11.7 1.0
OD1 A:ASP65 4.8 11.6 1.0
ND1 A:HIS145 4.9 9.2 1.0
CD2 A:HIS135 4.9 7.9 1.0
O A:GLY22 4.9 8.6 1.0
CA A:GLY22 5.0 9.8 1.0

Zinc binding site 2 out of 6 in 7qta

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Zinc binding site 2 out of 6 in the S1 Nuclease From Aspergillus Oryzae in Complex with Uridine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of S1 Nuclease From Aspergillus Oryzae in Complex with Uridine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn402

b:9.0
occ:1.00
O A:HOH670 1.9 6.6 0.5
O4 A:PO4406 2.0 12.2 0.3
OD2 A:ASP139 2.0 8.2 1.0
O4 A:PO4406 2.0 9.5 0.2
ND1 A:HIS80 2.1 8.8 1.0
NE2 A:HIS135 2.1 8.4 1.0
OD1 A:ASP65 2.7 11.6 1.0
CE1 A:HIS80 2.9 9.3 1.0
CG A:ASP139 3.0 7.4 1.0
CD2 A:HIS135 3.0 7.9 1.0
P A:PO4406 3.0 12.0 0.3
CE1 A:HIS135 3.1 8.3 1.0
O3 A:PO4406 3.1 11.4 0.3
CG A:HIS80 3.2 9.3 1.0
P A:PO4406 3.2 11.3 0.2
OD1 A:ASP139 3.3 8.1 1.0
ZN A:ZN401 3.3 8.3 1.0
CG A:ASP65 3.5 11.7 1.0
O2 A:PO4406 3.5 12.3 0.2
CB A:HIS80 3.6 8.5 1.0
OD2 A:ASP65 3.6 12.5 1.0
O1 A:PO4406 3.8 12.5 0.2
O1 A:PO4406 3.9 11.9 0.3
NE2 A:HIS26 4.0 7.8 1.0
NE2 A:HIS80 4.1 10.1 1.0
CG A:HIS135 4.2 8.2 1.0
ND1 A:HIS135 4.2 8.6 1.0
CD2 A:HIS80 4.2 10.3 1.0
O2 A:PO4406 4.2 13.6 0.3
CE1 A:HIS145 4.3 9.3 1.0
NZ A:LYS68 4.3 23.4 1.0
CB A:ASP139 4.4 7.3 1.0
CE1 A:HIS26 4.4 7.7 1.0
O A:HOH519 4.5 13.6 0.5
O3 A:PO4406 4.5 8.2 0.2
CA A:HIS80 4.6 8.5 1.0
O2' A:URI407 4.8 20.5 0.8
CB A:ASP65 4.9 10.8 1.0
O A:TRP21 4.9 8.6 1.0
ND1 A:HIS145 4.9 9.2 1.0
CD2 A:HIS26 5.0 8.1 1.0

Zinc binding site 3 out of 6 in 7qta

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Zinc binding site 3 out of 6 in the S1 Nuclease From Aspergillus Oryzae in Complex with Uridine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of S1 Nuclease From Aspergillus Oryzae in Complex with Uridine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn403

b:10.9
occ:1.00
O2 A:PO4406 1.9 13.6 0.3
NE2 A:HIS168 2.0 9.3 1.0
O A:HOH519 2.0 13.6 0.5
NE2 A:HIS145 2.0 9.7 1.0
OD2 A:ASP172 2.1 13.5 1.0
O3 A:PO4406 2.2 8.2 0.2
O A:HOH697 2.2 5.8 0.2
OD1 A:ASP172 2.6 9.6 1.0
CG A:ASP172 2.7 9.4 1.0
O2 A:PO4406 2.9 12.3 0.2
CE1 A:HIS145 2.9 9.3 1.0
CD2 A:HIS168 3.0 9.8 1.0
CE1 A:HIS168 3.0 9.4 1.0
P A:PO4406 3.1 11.3 0.2
CD2 A:HIS145 3.1 9.1 1.0
P A:PO4406 3.3 12.0 0.3
O3 A:PO4406 3.8 11.4 0.3
O4' A:URI407 3.9 15.8 0.8
C1' A:URI407 4.0 14.5 0.8
C4' A:URI407 4.1 19.9 0.8
ND1 A:HIS145 4.1 9.2 1.0
O1 A:PO4406 4.1 12.5 0.2
N A:TRP21 4.1 8.8 1.0
CB A:ASP172 4.1 8.9 1.0
ND1 A:HIS168 4.2 9.5 1.0
CG A:HIS168 4.2 9.3 1.0
O1 A:PO4406 4.2 11.9 0.3
O4 A:PO4406 4.2 9.5 0.2
CG A:HIS145 4.2 7.9 1.0
O A:HOH620 4.2 21.0 1.0
O4 A:PO4406 4.2 12.2 0.3
O A:HOH501 4.3 14.1 0.2
NE2 A:GLN142 4.4 8.9 1.0
O A:HOH670 4.5 6.6 0.5
O A:HOH700 4.5 18.8 1.0
O2' A:URI407 4.5 20.5 0.8
O2 A:URI407 4.6 13.3 0.8
ZN A:ZN401 4.6 8.3 1.0
O5' A:URI407 4.7 26.9 0.8
CE1 A:PHE81 4.7 8.8 0.2
C2' A:URI407 4.8 16.5 0.8
CA A:TRP21 4.9 9.2 1.0
O A:TRP21 4.9 8.6 1.0
C A:TRP21 5.0 8.0 1.0

Zinc binding site 4 out of 6 in 7qta

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Zinc binding site 4 out of 6 in the S1 Nuclease From Aspergillus Oryzae in Complex with Uridine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of S1 Nuclease From Aspergillus Oryzae in Complex with Uridine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn401

b:8.9
occ:1.00
O2 B:PO4406 1.9 10.1 0.3
O3 B:PO4406 1.9 9.4 0.2
NE2 B:HIS26 2.0 8.2 1.0
O B:HOH1093 2.0 8.6 0.5
OD1 B:ASP139 2.1 8.2 1.0
N B:TRP21 2.1 9.2 1.0
O B:TRP21 2.2 9.0 1.0
C B:TRP21 2.9 8.6 1.0
CA B:TRP21 3.0 9.3 1.0
CE1 B:HIS26 3.0 8.3 1.0
CD2 B:HIS26 3.0 8.5 1.0
P B:PO4406 3.0 11.1 0.3
CG B:ASP139 3.1 7.9 1.0
P B:PO4406 3.2 8.8 0.2
O3 B:PO4406 3.2 12.5 0.3
ZN B:ZN402 3.4 9.4 1.0
O B:HOH931 3.5 19.4 0.5
OD2 B:ASP139 3.5 9.6 1.0
O2 B:PO4406 3.6 9.3 0.2
CB B:TRP21 3.7 9.0 1.0
O1 B:PO4406 3.7 11.6 0.2
O1 B:PO4406 3.8 13.1 0.3
NE2 B:HIS135 3.9 9.0 1.0
OD2 B:ASP65 3.9 13.3 1.0
CE1 B:HIS135 4.1 9.2 1.0
CE1 B:HIS145 4.1 9.8 1.0
ND1 B:HIS26 4.1 8.3 1.0
CG B:HIS26 4.2 8.4 1.0
O4 B:PO4406 4.2 12.5 0.3
N B:GLY22 4.2 9.8 1.0
NE2 B:HIS145 4.3 10.0 1.0
CG B:TRP21 4.4 9.0 1.0
CB B:ASP139 4.4 8.1 1.0
O4 B:PO4406 4.4 8.0 0.2
CD1 B:TRP21 4.4 9.4 1.0
ZN B:ZN403 4.6 11.3 1.0
OD1 B:ASP172 4.6 10.0 1.0
CA B:ASP139 4.7 7.7 1.0
CG B:ASP65 4.8 12.0 1.0
OD1 B:ASP65 4.8 12.3 1.0
CD2 B:HIS135 4.9 9.0 1.0
O B:GLY22 4.9 9.0 1.0
ND1 B:HIS145 4.9 9.2 1.0
CA B:GLY22 5.0 9.4 1.0

Zinc binding site 5 out of 6 in 7qta

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Zinc binding site 5 out of 6 in the S1 Nuclease From Aspergillus Oryzae in Complex with Uridine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of S1 Nuclease From Aspergillus Oryzae in Complex with Uridine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn402

b:9.4
occ:1.00
O B:HOH1093 1.9 8.6 0.5
OD2 B:ASP139 2.0 9.6 1.0
ND1 B:HIS80 2.0 9.6 1.0
NE2 B:HIS135 2.0 9.0 1.0
O2 B:PO4406 2.1 9.3 0.2
O2 B:PO4406 2.1 10.1 0.3
OD1 B:ASP65 2.7 12.3 1.0
CE1 B:HIS80 2.9 10.3 1.0
CG B:ASP139 3.0 7.9 1.0
CD2 B:HIS135 3.0 9.0 1.0
O4 B:PO4406 3.0 12.5 0.3
CE1 B:HIS135 3.1 9.2 1.0
P B:PO4406 3.1 11.1 0.3
CG B:HIS80 3.1 10.0 1.0
P B:PO4406 3.2 8.8 0.2
OD1 B:ASP139 3.3 8.2 1.0
ZN B:ZN401 3.4 8.9 1.0
O3 B:PO4406 3.5 9.4 0.2
CG B:ASP65 3.5 12.0 1.0
CB B:HIS80 3.6 9.7 1.0
OD2 B:ASP65 3.7 13.3 1.0
O1 B:PO4406 3.8 11.6 0.2
O1 B:PO4406 4.0 13.1 0.3
NE2 B:HIS26 4.0 8.2 1.0
NE2 B:HIS80 4.1 10.8 1.0
CG B:HIS135 4.2 8.8 1.0
CD2 B:HIS80 4.2 10.5 1.0
ND1 B:HIS135 4.2 9.4 1.0
O3 B:PO4406 4.3 12.5 0.3
CB B:ASP139 4.3 8.1 1.0
CE1 B:HIS145 4.3 9.8 1.0
NZ B:LYS68 4.4 24.6 1.0
CE1 B:HIS26 4.4 8.3 1.0
O B:HOH931 4.5 19.4 0.5
O4 B:PO4406 4.5 8.0 0.2
CA B:HIS80 4.6 8.9 1.0
CB B:ASP65 4.9 11.2 1.0
O B:TRP21 4.9 9.0 1.0
O2' B:URI407 4.9 16.8 0.8
ND1 B:HIS145 5.0 9.2 1.0
CD2 B:HIS26 5.0 8.5 1.0

Zinc binding site 6 out of 6 in 7qta

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Zinc binding site 6 out of 6 in the S1 Nuclease From Aspergillus Oryzae in Complex with Uridine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of S1 Nuclease From Aspergillus Oryzae in Complex with Uridine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn403

b:11.3
occ:1.00
O3 B:PO4406 1.8 12.5 0.3
O B:HOH931 2.0 19.4 0.5
NE2 B:HIS168 2.0 9.4 1.0
NE2 B:HIS145 2.0 10.0 1.0
OD2 B:ASP172 2.1 13.5 1.0
O4 B:PO4406 2.2 8.0 0.2
O B:HOH1154 2.3 6.7 0.2
OD1 B:ASP172 2.6 10.0 1.0
CG B:ASP172 2.7 10.0 1.0
O3 B:PO4406 2.9 9.4 0.2
CE1 B:HIS145 2.9 9.8 1.0
CD2 B:HIS168 3.0 10.0 1.0
CE1 B:HIS168 3.1 9.8 1.0
P B:PO4406 3.1 8.8 0.2
CD2 B:HIS145 3.1 9.2 1.0
P B:PO4406 3.2 11.1 0.3
O4 B:PO4406 3.7 12.5 0.3
O4' B:URI407 4.0 14.4 0.8
C4' B:URI407 4.0 18.2 0.8
C1' B:URI407 4.1 13.8 0.8
O1 B:PO4406 4.1 13.1 0.3
ND1 B:HIS145 4.1 9.2 1.0
N B:TRP21 4.1 9.2 1.0
CB B:ASP172 4.1 9.0 1.0
O1 B:PO4406 4.1 11.6 0.2
O2 B:PO4406 4.2 9.3 0.2
ND1 B:HIS168 4.2 9.8 1.0
O B:HOH1054 4.2 20.7 1.0
O2 B:PO4406 4.2 10.1 0.3
CG B:HIS168 4.2 9.6 1.0
CG B:HIS145 4.2 8.7 1.0
NE2 B:GLN142 4.4 9.4 1.0
O B:HOH1093 4.5 8.6 0.5
O B:HOH1120 4.5 20.1 1.0
O2' B:URI407 4.5 16.8 0.8
ZN B:ZN401 4.6 8.9 1.0
O5' B:URI407 4.6 25.5 0.8
O2 B:URI407 4.7 12.5 0.8
C2' B:URI407 4.8 15.6 0.8
CA B:TRP21 4.8 9.3 1.0
O B:TRP21 4.9 9.0 1.0
CE2 B:PHE81 4.9 17.4 0.2
C B:TRP21 4.9 8.6 1.0
C5' B:URI407 5.0 19.8 0.8

Reference:

K.Adamkova, T.Koval', L.H.Ostergaard, J.Duskova, M.Maly, L.Svecova, T.Skalova, P.Kolenko, J.Dohnalek. Atomic Resolution Studies of S1 Nuclease Complexes Reveal Details of Rna Interaction with the Enzyme Despite Multiple Lattice-Translocation Defects. Acta Crystallogr D Struct V. 78 1194 2022BIOL.
ISSN: ISSN 2059-7983
PubMed: 36189740
DOI: 10.1107/S2059798322008397
Page generated: Wed Oct 30 10:03:24 2024

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