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Zinc in PDB 6ruw: Zn-Substituted Alpha-Keggin Bound to Proteinase K Solved By Mr

Enzymatic activity of Zn-Substituted Alpha-Keggin Bound to Proteinase K Solved By Mr

All present enzymatic activity of Zn-Substituted Alpha-Keggin Bound to Proteinase K Solved By Mr:
3.4.21.64;

Protein crystallography data

The structure of Zn-Substituted Alpha-Keggin Bound to Proteinase K Solved By Mr, PDB code: 6ruw was solved by J.Breibeck, A.Bijelic, A.Rompel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.04 / 1.35
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 67.920, 67.920, 102.140, 90.00, 90.00, 90.00
R / Rfree (%) 14.8 / 18.1

Other elements in 6ruw:

The structure of Zn-Substituted Alpha-Keggin Bound to Proteinase K Solved By Mr also contains other interesting chemical elements:

Tungsten (W) 11 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Zn-Substituted Alpha-Keggin Bound to Proteinase K Solved By Mr (pdb code 6ruw). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Zn-Substituted Alpha-Keggin Bound to Proteinase K Solved By Mr, PDB code: 6ruw:

Zinc binding site 1 out of 1 in 6ruw

Go back to Zinc Binding Sites List in 6ruw
Zinc binding site 1 out of 1 in the Zn-Substituted Alpha-Keggin Bound to Proteinase K Solved By Mr


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Zn-Substituted Alpha-Keggin Bound to Proteinase K Solved By Mr within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:97.8
occ:0.64
ZN1 A:KK5301 0.0 97.8 0.6
O76 A:KK5301 2.1 97.9 0.6
O77 A:KK5301 2.1 97.9 0.6
O75 A:KK5301 2.2 97.7 0.6
O78 A:KK5301 2.2 97.7 0.6
O61 A:KK5301 2.7 97.7 0.6
HG A:SER63 3.0 16.4 0.5
HG3 A:MET55 3.2 7.3 1.0
HG2 A:MET55 3.4 7.3 1.0
HA A:ARG64 3.4 11.2 1.0
W17 A:KK5301 3.5 97.7 0.6
W18 A:KK5301 3.6 97.3 0.6
P2 A:KK5301 3.6 97.7 0.6
W12 A:KK5301 3.7 97.4 0.6
W13 A:KK5301 3.7 97.7 0.6
CG A:MET55 3.8 6.1 1.0
O55 A:KK5301 3.8 97.7 0.6
O41 A:KK5301 3.8 97.7 0.6
OG A:SER63 3.8 13.7 0.5
O59 A:KK5301 3.9 97.6 0.6
O60 A:KK5301 3.9 97.8 0.6
O53 A:KK5301 4.0 97.9 0.6
O57 A:KK5301 4.0 97.5 0.6
O A:ILE42 4.1 6.1 1.0
H A:ALA44 4.1 8.8 1.0
HB2 A:MET55 4.1 6.6 1.0
HB2 A:SER63 4.1 13.6 0.5
HB2 A:ARG64 4.1 15.3 1.0
CA A:ARG64 4.2 9.4 1.0
O A:HOH636 4.2 11.1 1.0
O A:SER63 4.3 7.5 1.0
N A:ARG64 4.4 8.4 1.0
O46 A:KK5301 4.4 97.6 0.6
HB3 A:ALA44 4.4 10.2 1.0
C A:SER63 4.4 8.1 1.0
O45 A:KK5301 4.5 97.9 0.6
CB A:MET55 4.5 5.5 1.0
HB3 A:SER63 4.5 13.6 0.5
HA A:GLU43 4.6 7.3 1.0
O40 A:KK5301 4.6 97.6 0.6
O42 A:KK5301 4.7 98.0 0.6
CB A:ARG64 4.7 12.8 1.0
CB A:SER63 4.8 11.3 0.5
H A:ARG64 4.8 10.1 1.0
HB2 A:SER63 4.8 13.6 0.5
CB A:SER63 4.8 11.3 0.5
O54 A:KK5301 4.8 97.9 0.6
O56 A:KK5301 4.9 97.6 0.6
H A:MET55 4.9 7.8 1.0
N A:ALA44 4.9 7.3 1.0
H A:ASP65 5.0 8.3 1.0

Reference:

J.Breibeck, A.Bijelic, A.Rompel. Transition Metal-Substituted Keggin Polyoxotungstates Enabling Covalent Attachment to Proteinase K Upon Co-Crystallization. Chem.Commun.(Camb.) V. 55 11519 2019.
ISSN: ESSN 1364-548X
PubMed: 31490500
DOI: 10.1039/C9CC05818D
Page generated: Wed Dec 16 12:42:37 2020

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