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Zinc in PDB 1yqy: Structure of B. Anthrax Lethal Factor in Complex with A Hydroxamate Inhibitor

Enzymatic activity of Structure of B. Anthrax Lethal Factor in Complex with A Hydroxamate Inhibitor

All present enzymatic activity of Structure of B. Anthrax Lethal Factor in Complex with A Hydroxamate Inhibitor:
3.4.24.83;

Protein crystallography data

The structure of Structure of B. Anthrax Lethal Factor in Complex with A Hydroxamate Inhibitor, PDB code: 1yqy was solved by W.L.Shoop, Y.Xiong, J.Wiltsie, A.Woods, J.Guo, J.V.Pivnichny, T.Felcetto, B.F.Michael, A.Bansal, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 57.332, 75.957, 139.006, 90.00, 90.00, 90.00
R / Rfree (%) 19.1 / 26.9

Other elements in 1yqy:

The structure of Structure of B. Anthrax Lethal Factor in Complex with A Hydroxamate Inhibitor also contains other interesting chemical elements:

Fluorine (F) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of B. Anthrax Lethal Factor in Complex with A Hydroxamate Inhibitor (pdb code 1yqy). 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 Structure of B. Anthrax Lethal Factor in Complex with A Hydroxamate Inhibitor, PDB code: 1yqy:

Zinc binding site 1 out of 1 in 1yqy

Go back to Zinc Binding Sites List in 1yqy
Zinc binding site 1 out of 1 in the Structure of B. Anthrax Lethal Factor in Complex with A Hydroxamate Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of B. Anthrax Lethal Factor in Complex with A Hydroxamate Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn781

b:25.4
occ:1.00
 NE2 A:HIS690 2.1 27.1 1.0
NE2 A:HIS686 2.1 28.1 1.0
O21 A:915782 2.2 30.2 1.0
OE1 A:GLU735 2.3 42.5 1.0
O20 A:915782 2.4 27.2 1.0
CE1 A:HIS686 3.0 28.7 1.0
C18 A:915782 3.0 28.4 1.0
CE1 A:HIS690 3.0 26.4 1.0
CD2 A:HIS690 3.1 27.6 1.0
N19 A:915782 3.1 28.9 1.0
CD2 A:HIS686 3.1 28.7 1.0
CD A:GLU735 3.2 47.6 1.0
OE2 A:GLU735 3.3 36.2 1.0
O A:HOH793 4.0 18.3 1.0
ND1 A:HIS686 4.1 29.5 1.0
ND1 A:HIS690 4.1 26.9 1.0
CG A:HIS690 4.2 25.2 1.0
OE2 A:GLU687 4.2 15.5 1.0
CG A:HIS686 4.2 27.3 1.0
C17 A:915782 4.5 26.5 1.0
OH A:TYR728 4.5 32.1 1.0
CE2 A:TYR728 4.5 34.3 1.0
CB A:ALA738 4.5 24.6 1.0
CG A:GLU735 4.6 29.4 1.0
OE1 A:GLU687 4.7 20.4 1.0
O A:HOH1127 4.7 30.6 1.0
CA A:GLU735 4.8 20.3 1.0
CD A:GLU687 4.8 30.5 1.0
C33 A:915782 4.8 21.8 1.0
CB A:GLU735 4.9 21.0 1.0
C27 A:915782 4.9 22.6 1.0

Reference:

W.L.Shoop, Y.Xiong, J.Wiltsie, A.Woods, J.Guo, J.V.Pivnichny, T.Felcetto, B.F.Michael, A.Bansal, R.T.Cummings, B.R.Cunningham, A.M.Friedlander, C.M.Douglas, S.B.Patel, D.Wisniewski, G.Scapin, S.P.Salowe, D.M.Zaller, K.T.Chapman, E.M.Scolnick, D.M.Schmatz, K.Bartizal, M.Maccoss, J.D.Hermes. Anthrax Lethal Factor Inhibition. Proc.Natl.Acad.Sci.Usa V. 102 7958 2005.
ISSN: ISSN 0027-8424
PubMed: 15911756
DOI: 10.1073/PNAS.0502159102
Page generated: Wed Oct 16 21:03:30 2024

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