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Calcium in PDB 2wqd: Crystal Structure of Enzyme I of the Phosphoenolpyruvate:Sugar Phosphotransferase System in the Dephosphorylated State

Protein crystallography data

The structure of Crystal Structure of Enzyme I of the Phosphoenolpyruvate:Sugar Phosphotransferase System in the Dephosphorylated State, PDB code: 2wqd was solved by A.E.Oberholzer, P.Schneider, C.Siebold, U.Baumann, B.Erni, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.906 / 2.40
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 98.340, 98.340, 105.110, 90.00, 90.00, 120.00
R / Rfree (%) 22.82 / 29.51

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Enzyme I of the Phosphoenolpyruvate:Sugar Phosphotransferase System in the Dephosphorylated State (pdb code 2wqd). 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 Crystal Structure of Enzyme I of the Phosphoenolpyruvate:Sugar Phosphotransferase System in the Dephosphorylated State, PDB code: 2wqd:

Calcium binding site 1 out of 1 in 2wqd

Go back to Calcium Binding Sites List in 2wqd
Calcium binding site 1 out of 1 in the Crystal Structure of Enzyme I of the Phosphoenolpyruvate:Sugar Phosphotransferase System in the Dephosphorylated State


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Enzyme I of the Phosphoenolpyruvate:Sugar Phosphotransferase System in the Dephosphorylated State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1572

b:78.6
occ:1.00
OE1 A:GLN477 2.9 56.5 1.0
CE2 A:TYR474 4.0 74.7 1.0
CD A:GLN477 4.0 49.3 1.0
CD2 A:TYR474 4.1 73.8 1.0
CD2 A:LEU475 4.5 54.3 1.0
NE2 A:GLN477 4.5 39.9 1.0
O A:HOH2151 4.9 32.3 1.0

Reference:

A.E.Oberholzer, P.Schneider, C.Siebold, U.Baumann, B.Erni. Crystal Structure of Enzyme I of the Phosphoenolpyruvate:Sugar Phosphotransferase System in the Dephosphorylated State. J.Biol.Chem. V. 284 33169 2009.
ISSN: ISSN 0021-9258
PubMed: 19801641
DOI: 10.1074/JBC.M109.057612
Page generated: Fri Jul 12 18:50:23 2024

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