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Zinc in PDB 2pu0: Crystal Structure of the T. Brucei Enolase Complexed with Phosphonoacetohydroxamate (Pah), HIS156-in Conformation

Enzymatic activity of Crystal Structure of the T. Brucei Enolase Complexed with Phosphonoacetohydroxamate (Pah), HIS156-in Conformation

All present enzymatic activity of Crystal Structure of the T. Brucei Enolase Complexed with Phosphonoacetohydroxamate (Pah), HIS156-in Conformation:
4.2.1.11;

Protein crystallography data

The structure of Crystal Structure of the T. Brucei Enolase Complexed with Phosphonoacetohydroxamate (Pah), HIS156-in Conformation, PDB code: 2pu0 was solved by M.V.A.S.Navarro, D.J.Rigden, R.C.Garratt, S.M.G.Dias, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 17.72 / 1.90
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 74.946, 110.760, 109.219, 90.00, 90.00, 90.00
R / Rfree (%) 16.5 / 20.5

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the T. Brucei Enolase Complexed with Phosphonoacetohydroxamate (Pah), HIS156-in Conformation (pdb code 2pu0). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Crystal Structure of the T. Brucei Enolase Complexed with Phosphonoacetohydroxamate (Pah), HIS156-in Conformation, PDB code: 2pu0:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in 2pu0

Go back to Zinc Binding Sites List in 2pu0
Zinc binding site 1 out of 3 in the Crystal Structure of the T. Brucei Enolase Complexed with Phosphonoacetohydroxamate (Pah), HIS156-in Conformation


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 the T. Brucei Enolase Complexed with Phosphonoacetohydroxamate (Pah), HIS156-in Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:21.3
occ:1.00
 OE2 A:GLU291 2.0 15.6 1.0
O A:HOH940 2.0 15.1 1.0
O3 A:PAH600 2.0 26.6 1.0
OD2 A:ASP318 2.2 17.1 1.0
OD2 A:ASP243 2.2 18.2 1.0
O2 A:PAH600 2.5 20.5 1.0
N3 A:PAH600 3.0 25.4 1.0
CG A:ASP243 3.1 18.5 1.0
CD A:GLU291 3.1 16.9 1.0
C2 A:PAH600 3.1 23.7 1.0
CG A:ASP318 3.2 15.6 1.0
OD1 A:ASP243 3.3 16.4 1.0
CB A:ASP318 3.6 15.2 1.0
NZ A:LYS394 3.8 17.0 1.0
OE1 A:GLU291 3.8 17.8 1.0
NZ A:LYS343 3.9 15.9 1.0
O A:HOH938 3.9 17.1 1.0
O A:HOH941 4.0 19.5 1.0
OD2 A:ASP292 4.0 17.3 1.0
CG A:GLU291 4.0 18.7 1.0
ZN A:ZN502 4.1 24.4 1.0
OE1 A:GLN164 4.2 22.6 1.0
CD2 A:LEU341 4.2 15.4 1.0
OD1 A:ASP318 4.2 20.1 1.0
CB A:ASP243 4.4 19.8 1.0
C1 A:PAH600 4.6 18.1 1.0
OE2 A:GLU165 4.7 22.2 1.0
CG A:ASP292 4.9 19.4 1.0
CE A:LYS394 4.9 15.9 1.0
CB A:ALA245 5.0 22.1 1.0

Zinc binding site 2 out of 3 in 2pu0

Go back to Zinc Binding Sites List in 2pu0
Zinc binding site 2 out of 3 in the Crystal Structure of the T. Brucei Enolase Complexed with Phosphonoacetohydroxamate (Pah), HIS156-in Conformation


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 the T. Brucei Enolase Complexed with Phosphonoacetohydroxamate (Pah), HIS156-in Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn502

b:24.4
occ:1.00
 O A:SER40 2.1 22.3 1.0
O2P A:PAH600 2.1 18.2 1.0
O A:HOH938 2.2 17.1 1.0
O A:HOH941 2.2 19.5 1.0
O2 A:PAH600 2.2 20.5 1.0
OG A:SER40 2.2 19.9 1.0
C2 A:PAH600 3.0 23.7 1.0
C A:SER40 3.1 21.6 1.0
CB A:SER40 3.2 21.5 1.0
P A:PAH600 3.4 18.2 1.0
C1 A:PAH600 3.5 18.1 1.0
CA A:SER40 3.5 21.5 1.0
OD2 A:ASP318 3.8 17.1 1.0
OD2 A:ASP319 3.9 19.9 1.0
NZ A:LYS343 4.0 15.9 1.0
O3P A:PAH600 4.0 18.8 1.0
N A:SER40 4.0 20.7 1.0
OD1 A:ASP319 4.1 21.1 1.0
ZN A:ZN501 4.1 21.3 1.0
N3 A:PAH600 4.1 25.4 1.0
NH2 A:ARG372 4.1 13.0 1.0
O A:HOH940 4.2 15.1 1.0
N A:THR41 4.3 21.2 1.0
NE2 A:GLN164 4.3 19.4 1.0
OE1 A:GLN164 4.4 22.6 1.0
CG A:ASP319 4.4 18.3 1.0
O3 A:PAH600 4.5 26.6 1.0
O1P A:PAH600 4.6 21.0 1.0
CA A:THR41 4.7 20.1 1.0
CD A:GLN164 4.8 22.1 1.0
CG A:ASP318 4.9 15.6 1.0

Zinc binding site 3 out of 3 in 2pu0

Go back to Zinc Binding Sites List in 2pu0
Zinc binding site 3 out of 3 in the Crystal Structure of the T. Brucei Enolase Complexed with Phosphonoacetohydroxamate (Pah), HIS156-in Conformation


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of the T. Brucei Enolase Complexed with Phosphonoacetohydroxamate (Pah), HIS156-in Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn505

b:41.9
occ:0.70
 OE2 A:GLU27 2.0 30.0 1.0
ND1 A:HIS0 2.4 60.1 1.0
O A:HOH939 2.7 53.4 1.0
CD A:GLU27 2.8 31.1 1.0
OE1 A:GLU27 3.0 33.1 1.0
CE1 A:HIS0 3.2 61.3 1.0
CG A:HIS0 3.5 57.7 1.0
CB A:HIS0 3.9 54.4 1.0
CG A:GLU27 4.2 28.0 1.0
NE2 A:HIS0 4.4 61.7 1.0
O A:HIS0 4.5 50.2 1.0
CD2 A:HIS0 4.6 60.8 1.0
C A:HIS0 4.6 50.6 1.0
CG A:MET1 4.6 47.3 1.0
CB A:GLU27 4.6 25.8 1.0
CA A:HIS0 4.9 53.0 1.0

Reference:

M.V.Navarro, S.M.Gomes Dias, L.V.Mello, M.T.Da Silva Giotto, S.Gavalda, C.Blonski, R.C.Garratt, D.J.Rigden. Structural Flexibility in Trypanosoma Brucei Enolase Revealed By X-Ray Crystallography and Molecular Dynamics. Febs J. V. 274 5077 2007.
ISSN: ISSN 1742-464X
PubMed: 17822439
DOI: 10.1111/J.1742-4658.2007.06027.X
Page generated: Thu Oct 17 03:13:24 2024

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