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Magnesium in PDB 4f8e: Pyruvate Formate-Lyase (E.Coli) in Complex with Coa and the Substrate Analog Oxamate

Enzymatic activity of Pyruvate Formate-Lyase (E.Coli) in Complex with Coa and the Substrate Analog Oxamate

All present enzymatic activity of Pyruvate Formate-Lyase (E.Coli) in Complex with Coa and the Substrate Analog Oxamate:
2.3.1.54;

Protein crystallography data

The structure of Pyruvate Formate-Lyase (E.Coli) in Complex with Coa and the Substrate Analog Oxamate, PDB code: 4f8e was solved by A.Becker, W.Kabsch, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15 / 1.75
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 54.938, 153.169, 205.909, 90.00, 90.00, 90.00
R / Rfree (%) 14.8 / 17.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Pyruvate Formate-Lyase (E.Coli) in Complex with Coa and the Substrate Analog Oxamate (pdb code 4f8e). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Pyruvate Formate-Lyase (E.Coli) in Complex with Coa and the Substrate Analog Oxamate, PDB code: 4f8e:

Magnesium binding site 1 out of 1 in 4f8e

Go back to Magnesium Binding Sites List in 4f8e
Magnesium binding site 1 out of 1 in the Pyruvate Formate-Lyase (E.Coli) in Complex with Coa and the Substrate Analog Oxamate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Pyruvate Formate-Lyase (E.Coli) in Complex with Coa and the Substrate Analog Oxamate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg9008

b:60.7
occ:1.00
O5B A:COA1000 2.1 19.0 1.0
O5A A:COA1000 2.2 24.5 1.0
O A:HOH3246 2.7 41.1 1.0
O A:HOH2491 2.8 42.2 1.0
C5B A:COA1000 2.8 16.7 1.0
P1A A:COA1000 3.0 22.0 1.0
P2A A:COA1000 3.1 22.9 1.0
O3A A:COA1000 3.1 22.1 1.0
O1A A:COA1000 3.2 23.4 1.0
C3B A:COA1000 3.6 17.8 1.0
C4B A:COA1000 3.6 16.9 1.0
O6A A:COA1000 3.8 20.9 1.0
O A:HOH3239 3.9 56.3 1.0
C2B A:COA1000 4.0 16.8 1.0
NZ A:LYS161 4.4 23.7 1.0
O4A A:COA1000 4.4 25.3 1.0
O2A A:COA1000 4.4 22.4 1.0
O7A A:COA1000 4.6 24.1 1.0
O2B A:COA1000 4.8 17.4 1.0
O4B A:COA1000 4.8 15.5 1.0
O3B A:COA1000 4.8 19.9 1.0
N3A A:COA1000 4.8 13.6 1.0

Reference:

A.Becker, W.Kabsch. X-Ray Structure of Pyruvate Formate-Lyase in Complex with Pyruvate and Coa.How the Enzyme Uses the Cys-418 Thiyl Radical For Pyruvate Cleavage J.Biol.Chem. V. 277 40036 2002.
ISSN: ISSN 0021-9258
PubMed: 12163496
DOI: 10.1074/JBC.M205821200
Page generated: Fri Aug 16 14:44:52 2024

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