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Magnesium in PDB 3dgb: Crystal Structure of Muconate Lactonizing Enzyme From Pseudomonas Fluorescens Complexed with Muconolactone

Enzymatic activity of Crystal Structure of Muconate Lactonizing Enzyme From Pseudomonas Fluorescens Complexed with Muconolactone

All present enzymatic activity of Crystal Structure of Muconate Lactonizing Enzyme From Pseudomonas Fluorescens Complexed with Muconolactone:
5.5.1.1;

Protein crystallography data

The structure of Crystal Structure of Muconate Lactonizing Enzyme From Pseudomonas Fluorescens Complexed with Muconolactone, PDB code: 3dgb was solved by A.A.Fedorov, E.V.Fedorov, J.M.Sauder, S.K.Burley, J.A.Gerlt, S.C.Almo, Newyork Sgx Research Center For Structural Genomics (Nysgxrc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.93 / 1.70
Space group I 4 2 2
Cell size a, b, c (Å), α, β, γ (°) 133.842, 133.842, 103.371, 90.00, 90.00, 90.00
R / Rfree (%) 18.9 / 20.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Muconate Lactonizing Enzyme From Pseudomonas Fluorescens Complexed with Muconolactone (pdb code 3dgb). 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 Crystal Structure of Muconate Lactonizing Enzyme From Pseudomonas Fluorescens Complexed with Muconolactone, PDB code: 3dgb:

Magnesium binding site 1 out of 1 in 3dgb

Go back to Magnesium Binding Sites List in 3dgb
Magnesium binding site 1 out of 1 in the Crystal Structure of Muconate Lactonizing Enzyme From Pseudomonas Fluorescens Complexed with Muconolactone


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Muconate Lactonizing Enzyme From Pseudomonas Fluorescens Complexed with Muconolactone within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg2001

b:17.1
occ:1.00
 O A:HOH2237 1.8 22.7 1.0
OD2 A:ASP251 2.2 19.3 1.0
OE2 A:GLU226 2.3 16.9 1.0
OD2 A:ASP200 2.3 20.1 1.0
O1 A:MUC1001 2.4 30.7 1.0
O2 A:MUC1001 3.0 33.6 1.0
C1 A:MUC1001 3.0 31.9 1.0
CD A:GLU226 3.2 16.5 1.0
CG A:ASP200 3.2 18.9 1.0
CG A:ASP251 3.3 18.9 1.0
OD1 A:ASP200 3.3 17.9 1.0
ND2 A:ASN202 3.5 21.5 1.0
CB A:ASP251 3.7 15.0 1.0
OE1 A:GLU252 3.7 17.4 1.0
CG A:GLU226 3.9 12.6 1.0
O A:HOH2236 3.9 27.9 1.0
OH A:TYR61 3.9 26.3 1.0
OE1 A:GLU226 3.9 16.6 1.0
NZ A:LYS169 4.0 20.6 1.0
NZ A:LYS275 4.0 19.1 1.0
OE2 A:GLU252 4.2 23.9 1.0
CD A:GLU252 4.2 20.8 1.0
NZ A:LYS171 4.3 27.9 1.0
OD1 A:ASP251 4.4 19.4 1.0
C2 A:MUC1001 4.4 28.8 1.0
CG A:ASN202 4.5 21.0 1.0
CB A:ASP200 4.6 16.2 1.0
CE A:LYS169 4.8 20.2 1.0
OD1 A:ASN202 4.9 23.5 1.0

Reference:

A.Sakai, A.A.Fedorov, E.V.Fedorov, A.M.Schnoes, M.E.Glasner, S.Brown, M.E.Rutter, K.Bain, S.Chang, T.Gheyi, J.M.Sauder, S.K.Burley, P.C.Babbitt, S.C.Almo, J.A.Gerlt. Evolution of Enzymatic Activities in the Enolase Superfamily: Stereochemically Distinct Mechanisms in Two Families of Cis,Cis-Muconate Lactonizing Enzymes Biochemistry V. 48 1445 2009.
ISSN: ISSN 0006-2960
PubMed: 19220063
DOI: 10.1021/BI802277H
Page generated: Wed Aug 14 12:30:06 2024

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