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

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

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

Protein crystallography data

The structure of Crystal Structure of the T. Brucei Enolase Complexed with Phosphonoacetohydroxamate (Pah), HIS156-Out Conformation, PDB code: 2ptz 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) 27.95 / 1.65
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 73.858, 109.279, 107.946, 90.00, 90.00, 90.00
R / Rfree (%) 16.5 / 20.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the T. Brucei Enolase Complexed with Phosphonoacetohydroxamate (Pah), HIS156-Out Conformation (pdb code 2ptz). 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-Out Conformation, PDB code: 2ptz:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in 2ptz

Go back to Zinc Binding Sites List in 2ptz
Zinc binding site 1 out of 3 in the Crystal Structure of the T. Brucei Enolase Complexed with Phosphonoacetohydroxamate (Pah), HIS156-Out 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-Out Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn500

b:23.6
occ:1.00
 OE2 A:GLU291 2.0 19.9 1.0
OD2 A:ASP243 2.1 18.6 1.0
OD2 A:ASP318 2.1 18.3 1.0
O3 A:PAH600 2.2 19.1 1.0
O A:HOH1112 2.2 21.1 1.0
O2 A:PAH600 2.4 18.5 1.0
N3 A:PAH600 2.9 18.4 1.0
CG A:ASP243 2.9 21.1 1.0
C2 A:PAH600 3.0 18.2 1.0
CD A:GLU291 3.0 19.9 1.0
CG A:ASP318 3.1 20.2 1.0
OD1 A:ASP243 3.2 22.0 1.0
NZ A:LYS394 3.5 18.3 1.0
CB A:ASP318 3.6 20.8 1.0
OE1 A:GLU291 3.7 22.5 1.0
NZ A:LYS343 3.7 19.1 1.0
O A:HOH727 3.9 25.3 1.0
O A:HOH1100 4.0 23.2 1.0
OE1 A:GLN164 4.0 27.5 1.0
CD2 A:LEU341 4.0 21.3 1.0
ZN A:ZN501 4.1 24.3 1.0
OD2 A:ASP292 4.1 22.9 1.0
OD1 A:ASP318 4.1 20.3 1.0
CG A:GLU291 4.1 20.8 1.0
CB A:ASP243 4.3 23.7 1.0
C1 A:PAH600 4.5 19.6 1.0
OE2 A:GLU165 4.6 22.0 1.0
CE A:LYS394 4.8 19.0 1.0
CE A:LYS343 4.9 16.8 1.0
CG A:ASP292 4.9 23.7 1.0

Zinc binding site 2 out of 3 in 2ptz

Go back to Zinc Binding Sites List in 2ptz
Zinc binding site 2 out of 3 in the Crystal Structure of the T. Brucei Enolase Complexed with Phosphonoacetohydroxamate (Pah), HIS156-Out 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-Out Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:24.3
occ:1.00
 O2P A:PAH600 2.0 22.1 1.0
O A:SER40 2.1 21.6 1.0
O2 A:PAH600 2.1 18.5 1.0
O A:HOH1100 2.2 23.2 1.0
OG A:SER40 2.2 19.3 1.0
O A:HOH727 2.2 25.3 1.0
C2 A:PAH600 2.9 18.2 1.0
C A:SER40 2.9 21.4 1.0
CB A:SER40 3.0 21.6 1.0
P A:PAH600 3.1 20.6 1.0
C1 A:PAH600 3.3 19.6 1.0
CA A:SER40 3.4 22.1 1.0
OD2 A:ASP318 3.8 18.3 1.0
OD2 A:ASP319 3.9 23.4 1.0
N A:SER40 3.9 21.9 1.0
O3P A:PAH600 3.9 19.5 1.0
N3 A:PAH600 4.0 18.4 1.0
ZN A:ZN500 4.1 23.6 1.0
OD1 A:ASP319 4.1 23.9 1.0
N A:THR41 4.1 20.6 1.0
NH2 A:ARG372 4.1 18.3 1.0
NZ A:LYS343 4.1 19.1 1.0
O A:HOH1112 4.2 21.1 1.0
NE2 A:GLN164 4.3 20.6 1.0
O1P A:PAH600 4.3 18.4 1.0
OE1 A:GLN164 4.4 27.5 1.0
CG A:ASP319 4.4 20.4 1.0
O3 A:PAH600 4.5 19.1 1.0
CA A:THR41 4.6 21.2 1.0
CD A:GLN164 4.8 23.8 1.0
CG A:ASP318 4.9 20.2 1.0
CB A:ALA245 5.0 26.4 1.0

Zinc binding site 3 out of 3 in 2ptz

Go back to Zinc Binding Sites List in 2ptz
Zinc binding site 3 out of 3 in the Crystal Structure of the T. Brucei Enolase Complexed with Phosphonoacetohydroxamate (Pah), HIS156-Out 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-Out Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn550

b:35.8
occ:0.50
 OE2 A:GLU27 1.9 36.7 1.0
ND1 A:HIS0 2.6 57.9 1.0
O A:HOH939 2.6 48.7 1.0
CD A:GLU27 2.7 37.0 1.0
OE1 A:GLU27 2.9 39.2 1.0
CE1 A:HIS0 3.5 58.3 1.0
CG A:HIS0 3.5 56.5 1.0
CB A:HIS0 3.7 54.8 1.0
CG A:GLU27 4.1 32.9 1.0
O A:HIS0 4.4 49.3 1.0
CB A:GLU27 4.5 30.3 1.0
C A:HIS0 4.5 50.6 1.0
NE2 A:HIS0 4.6 58.1 1.0
CD2 A:HIS0 4.6 58.7 1.0
CA A:HIS0 4.7 53.3 1.0
CG A:MET1 4.8 48.7 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 03:13:15 2024

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