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Calcium in PDB 5enl: 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: 5enl 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

Calcium Binding Sites:

The binding sites of Calcium 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 5enl). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium 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: 5enl:

Calcium binding site 1 out of 1 in 5enl

Go back to Calcium Binding Sites List in 5enl
Calcium 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 Calcium with other atoms in the Ca 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:Ca438

b:25.5
occ:1.00
 O A:HOH449 2.1 5.6 1.0
OE2 A:GLU295 2.3 14.1 1.0
OD2 A:ASP320 2.3 13.8 1.0
O A:HOH514 2.5 81.3 1.0
OD2 A:ASP246 2.5 14.4 1.0
O A:HOH616 2.6 36.1 1.0
O3 A:2PG442 2.9 41.3 1.0
CG A:ASP246 3.2 13.7 1.0
OD1 A:ASP246 3.3 13.8 1.0
CD A:GLU295 3.3 13.2 1.0
CG A:ASP320 3.4 13.4 1.0
C3 A:2PG442 3.7 41.9 1.0
O A:HOH672 3.7 23.2 0.9
CB A:ASP320 3.8 12.9 1.0
NZ A:LYS396 4.0 11.0 1.0
OE1 A:GLU295 4.1 13.1 1.0
CG A:GLU295 4.2 11.8 1.0
OD2 A:ASP296 4.2 10.9 1.0
O A:HOH756 4.3 35.6 1.0
NE2 A:GLN167 4.5 17.2 1.0
CB A:ASP246 4.5 12.3 1.0
OD1 A:ASP320 4.5 13.3 1.0
OE2 A:GLU168 4.5 21.2 1.0
CD2 A:LEU343 4.6 7.6 1.0
O2 A:2PG442 4.7 42.6 1.0
NZ A:LYS345 4.7 10.0 1.0
C2 A:2PG442 4.9 42.0 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: Sat Dec 12 05:23:33 2020

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