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Zinc in PDB 6enl: Inhibition of Enolase: the Crystal Structures of Enolase-CA2+- Phosphoglycerate and Enolase-ZN2+-Phosphoglycolate Complexes at 2.2- Angstroms Resolution

Enzymatic activity of Inhibition of Enolase: the Crystal Structures of Enolase-CA2+- Phosphoglycerate and Enolase-ZN2+-Phosphoglycolate Complexes at 2.2- Angstroms Resolution

All present enzymatic activity of Inhibition of Enolase: the Crystal Structures of Enolase-CA2+- Phosphoglycerate and Enolase-ZN2+-Phosphoglycolate Complexes at 2.2- Angstroms Resolution:
4.2.1.11;

Protein crystallography data

The structure of Inhibition of Enolase: the Crystal Structures of Enolase-CA2+- Phosphoglycerate and Enolase-ZN2+-Phosphoglycolate Complexes at 2.2- Angstroms Resolution, PDB code: 6enl was solved by L.Lebioda, B.Stec, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 2.20
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 124.100, 124.100, 66.900, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Zinc Binding Sites:

The binding sites of Zinc atom in the Inhibition of Enolase: the Crystal Structures of Enolase-CA2+- Phosphoglycerate and Enolase-ZN2+-Phosphoglycolate Complexes at 2.2- Angstroms Resolution (pdb code 6enl). 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 Inhibition of Enolase: the Crystal Structures of Enolase-CA2+- Phosphoglycerate and Enolase-ZN2+-Phosphoglycolate Complexes at 2.2- Angstroms Resolution, PDB code: 6enl:

Zinc binding site 1 out of 1 in 6enl

Go back to Zinc Binding Sites List in 6enl
Zinc binding site 1 out of 1 in the Inhibition of Enolase: the Crystal Structures of Enolase-CA2+- Phosphoglycerate and Enolase-ZN2+-Phosphoglycolate Complexes at 2.2- Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Inhibition of Enolase: the Crystal Structures of Enolase-CA2+- Phosphoglycerate and Enolase-ZN2+-Phosphoglycolate Complexes at 2.2- Angstroms Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn438

b:15.6
occ:1.00
 O A:HOH446 1.7 3.0 1.0
OE2 A:GLU295 1.8 11.0 1.0
OD2 A:ASP320 2.1 12.5 1.0
OD2 A:ASP246 2.1 13.6 1.0
O2 A:PGA442 2.3 41.2 1.0
CD A:GLU295 2.8 10.7 1.0
CG A:ASP320 3.1 12.7 1.0
CG A:ASP246 3.1 13.7 1.0
OD1 A:ASP246 3.4 13.5 1.0
O A:HOH653 3.5 48.9 1.0
C1 A:PGA442 3.5 42.0 1.0
CB A:ASP320 3.5 12.7 1.0
NZ A:LYS396 3.6 12.1 1.0
OE1 A:GLU295 3.7 10.4 1.0
O1 A:PGA442 3.7 42.3 1.0
CG A:GLU295 3.8 10.2 1.0
O A:HOH667 4.0 25.6 1.0
OD2 A:ASP296 4.0 10.3 1.0
OD1 A:ASP320 4.2 13.0 1.0
CD2 A:LEU343 4.2 10.8 1.0
CB A:ASP246 4.4 13.3 1.0
OE2 A:GLU168 4.5 19.0 1.0
C2 A:PGA442 4.7 42.1 1.0
CG A:ASP296 4.8 10.9 1.0
NZ A:LYS345 4.8 13.5 1.0
NE2 A:GLN167 4.9 18.6 1.0
CE A:LYS396 4.9 11.9 1.0
CA A:ASP320 5.0 12.7 1.0
CB A:GLU295 5.0 9.7 1.0

Reference:

L.Lebioda, B.Stec, J.M.Brewer, E.Tykarska. Inhibition of Enolase: the Crystal Structures of Enolase-CA2(+)- 2-Phosphoglycerate and Enolase-ZN2(+)-Phosphoglycolate Complexes at 2.2-A Resolution. Biochemistry V. 30 2823 1991.
ISSN: ISSN 0006-2960
PubMed: 2007121
DOI: 10.1021/BI00225A013
Page generated: Mon Oct 28 20:15:17 2024

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