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Zinc in PDB 2pty: Crystal Structure of the T. Brucei Enolase Complexed with Pep

Enzymatic activity of Crystal Structure of the T. Brucei Enolase Complexed with Pep

All present enzymatic activity of Crystal Structure of the T. Brucei Enolase Complexed with Pep:
4.2.1.11;

Protein crystallography data

The structure of Crystal Structure of the T. Brucei Enolase Complexed with Pep, PDB code: 2pty 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) 24.98 / 2.00
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 73.991, 110.724, 109.304, 90.00, 90.00, 90.00
R / Rfree (%) 17.3 / 22.5

Zinc Binding Sites:

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

Zinc binding site 1 out of 2 in 2pty

Go back to Zinc Binding Sites List in 2pty
Zinc binding site 1 out of 2 in the Crystal Structure of the T. Brucei Enolase Complexed with Pep


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 Pep within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn500

b:33.9
occ:1.00
OE2 A:GLU291 1.9 31.7 1.0
O A:HOH745 2.2 25.8 1.0
OD2 A:ASP243 2.2 28.4 1.0
OD2 A:ASP318 2.2 31.1 1.0
O1 A:PEP600 2.2 36.3 1.0
O2' A:PEP600 2.3 28.6 1.0
C1 A:PEP600 2.6 30.5 1.0
CD A:GLU291 3.1 33.6 1.0
CG A:ASP243 3.1 29.0 1.0
CG A:ASP318 3.2 32.0 1.0
OD1 A:ASP243 3.4 31.3 1.0
CB A:ASP318 3.7 31.6 1.0
NZ A:LYS394 3.8 23.2 1.0
OE1 A:GLU291 3.9 34.0 1.0
NZ A:LYS343 3.9 25.6 1.0
OD2 A:ASP292 3.9 29.8 1.0
O A:HOH775 3.9 26.6 1.0
O A:HOH738 4.0 28.5 1.0
ZN A:ZN501 4.0 33.8 1.0
CG A:GLU291 4.0 32.5 1.0
CD2 A:LEU341 4.1 21.5 1.0
OE1 A:GLN164 4.1 30.9 1.0
C2 A:PEP600 4.1 32.0 1.0
OD1 A:ASP318 4.2 31.4 1.0
CB A:ASP243 4.4 32.0 1.0
OE2 A:GLU165 4.5 34.8 1.0
CG A:ASP292 4.8 34.1 1.0
CE A:LYS394 4.9 22.0 1.0
O2 A:PEP600 4.9 28.2 1.0
C3 A:PEP600 5.0 27.9 1.0
CE A:LYS343 5.0 24.5 1.0

Zinc binding site 2 out of 2 in 2pty

Go back to Zinc Binding Sites List in 2pty
Zinc binding site 2 out of 2 in the Crystal Structure of the T. Brucei Enolase Complexed with Pep


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 Pep within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:33.8
occ:1.00
O A:SER40 2.0 32.9 1.0
O A:HOH775 2.1 26.6 1.0
OG A:SER40 2.1 32.4 1.0
O A:HOH738 2.2 28.5 1.0
O1P A:PEP600 2.2 28.8 1.0
O2' A:PEP600 2.4 28.6 1.0
C A:SER40 3.0 32.5 1.0
CB A:SER40 3.2 32.8 1.0
C1 A:PEP600 3.4 30.5 1.0
P A:PEP600 3.4 25.4 1.0
O2 A:PEP600 3.5 28.2 1.0
CA A:SER40 3.6 32.5 1.0
OD2 A:ASP318 3.8 31.1 1.0
NZ A:LYS343 3.8 25.6 1.0
C2 A:PEP600 4.0 32.0 1.0
O2P A:PEP600 4.0 27.6 1.0
ZN A:ZN500 4.0 33.9 1.0
OD2 A:ASP319 4.0 29.6 1.0
O A:HOH745 4.1 25.8 1.0
OD1 A:ASP319 4.1 27.9 1.0
N A:SER40 4.1 31.8 1.0
N A:THR41 4.2 33.3 1.0
OE1 A:GLN164 4.3 30.9 1.0
NE2 A:GLN164 4.3 30.8 1.0
O1 A:PEP600 4.3 36.3 1.0
NH2 A:ARG372 4.3 24.6 1.0
CG A:ASP319 4.5 29.7 1.0
O3P A:PEP600 4.7 27.2 1.0
CA A:THR41 4.7 32.5 1.0
CD A:GLN164 4.7 31.8 1.0
CG A:ASP318 4.9 32.0 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: Wed Dec 16 03:49:05 2020

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