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Magnesium in PDB 5fjo: N-Acyl Amino Acid Racemase From Amycolatopsis Sp. Ts-1-60: G291D-F323Y Mutant in Complex with N-Acetyl Naphthylalanine

Enzymatic activity of N-Acyl Amino Acid Racemase From Amycolatopsis Sp. Ts-1-60: G291D-F323Y Mutant in Complex with N-Acetyl Naphthylalanine

All present enzymatic activity of N-Acyl Amino Acid Racemase From Amycolatopsis Sp. Ts-1-60: G291D-F323Y Mutant in Complex with N-Acetyl Naphthylalanine:
4.2.1.113;

Protein crystallography data

The structure of N-Acyl Amino Acid Racemase From Amycolatopsis Sp. Ts-1-60: G291D-F323Y Mutant in Complex with N-Acetyl Naphthylalanine, PDB code: 5fjo was solved by G.Sanchez-Carron, D.Campopiano, G.Grogan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 68.55 / 2.08
Space group I 4 2 2
Cell size a, b, c (Å), α, β, γ (°) 164.710, 164.710, 169.590, 90.00, 90.00, 90.00
R / Rfree (%) 14.456 / 17.465

Magnesium Binding Sites:

The binding sites of Magnesium atom in the N-Acyl Amino Acid Racemase From Amycolatopsis Sp. Ts-1-60: G291D-F323Y Mutant in Complex with N-Acetyl Naphthylalanine (pdb code 5fjo). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the N-Acyl Amino Acid Racemase From Amycolatopsis Sp. Ts-1-60: G291D-F323Y Mutant in Complex with N-Acetyl Naphthylalanine, PDB code: 5fjo:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 5fjo

Go back to Magnesium Binding Sites List in 5fjo
Magnesium binding site 1 out of 2 in the N-Acyl Amino Acid Racemase From Amycolatopsis Sp. Ts-1-60: G291D-F323Y Mutant in Complex with N-Acetyl Naphthylalanine


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of N-Acyl Amino Acid Racemase From Amycolatopsis Sp. Ts-1-60: G291D-F323Y Mutant in Complex with N-Acetyl Naphthylalanine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1369

b:17.7
occ:1.00
OD2 A:ASP239 2.3 17.2 1.0
OE2 A:GLU214 2.3 17.4 1.0
O A:HOH2295 2.4 14.0 1.0
OD2 A:ASP189 2.4 12.7 1.0
O A:NPQ1368 2.5 18.9 1.0
OXT A:NPQ1368 2.6 19.8 1.0
C A:NPQ1368 2.9 21.1 1.0
CD A:GLU214 3.0 16.4 1.0
CG A:ASP189 3.3 13.5 1.0
CG A:ASP239 3.4 15.2 1.0
OD1 A:ASP189 3.5 13.7 1.0
CB A:ASP239 3.7 12.9 1.0
NZ A:LYS161 3.7 15.4 1.0
ND2 A:ASN191 3.7 13.8 1.0
OE1 A:GLU214 3.7 16.7 1.0
CG A:GLU214 3.9 13.4 1.0
NZ A:LYS263 4.0 26.9 1.0
NZ A:LYS163 4.1 17.1 1.0
ND2 A:ASN261 4.2 19.1 1.0
OE1 A:GLU240 4.4 11.0 1.0
CA A:NPQ1368 4.5 23.8 1.0
OD1 A:ASP239 4.5 15.7 1.0
CG A:ASN191 4.5 14.6 1.0
O A:HOH2266 4.5 20.3 1.0
CB A:ASP189 4.6 12.6 1.0
CE A:LYS263 4.7 22.7 1.0
OD1 A:ASN191 4.7 16.5 1.0
CE A:LYS161 4.7 14.4 1.0
CB A:GLU214 5.0 12.1 1.0

Magnesium binding site 2 out of 2 in 5fjo

Go back to Magnesium Binding Sites List in 5fjo
Magnesium binding site 2 out of 2 in the N-Acyl Amino Acid Racemase From Amycolatopsis Sp. Ts-1-60: G291D-F323Y Mutant in Complex with N-Acetyl Naphthylalanine


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of N-Acyl Amino Acid Racemase From Amycolatopsis Sp. Ts-1-60: G291D-F323Y Mutant in Complex with N-Acetyl Naphthylalanine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1370

b:19.2
occ:1.00
O B:HOH2292 2.3 15.8 1.0
OD2 B:ASP239 2.3 17.5 1.0
OE2 B:GLU214 2.3 16.1 1.0
OD2 B:ASP189 2.4 16.4 1.0
O B:NPQ1369 2.5 21.5 1.0
OXT B:NPQ1369 2.6 17.2 1.0
C B:NPQ1369 2.9 21.2 1.0
CD B:GLU214 3.1 15.3 1.0
CG B:ASP189 3.3 16.7 1.0
CG B:ASP239 3.4 14.3 1.0
OD1 B:ASP189 3.5 16.9 1.0
NZ B:LYS161 3.7 18.9 1.0
CB B:ASP239 3.7 13.2 1.0
OE1 B:GLU214 3.7 16.2 1.0
ND2 B:ASN191 3.8 17.9 1.0
CG B:GLU214 3.9 13.8 1.0
NZ B:LYS263 4.0 23.0 1.0
NZ B:LYS163 4.1 21.4 1.0
ND2 B:ASN261 4.2 19.4 1.0
OE1 B:GLU240 4.4 12.8 1.0
O B:HOH2265 4.5 18.6 1.0
CA B:NPQ1369 4.5 25.8 1.0
OD1 B:ASP239 4.5 14.7 1.0
CG B:ASN191 4.6 17.7 1.0
CB B:ASP189 4.6 14.9 1.0
CE B:LYS263 4.6 18.1 1.0
CE B:LYS161 4.7 17.6 1.0
OD1 B:ASN191 4.8 18.2 1.0
CB B:GLU214 5.0 12.8 1.0

Reference:

G.Sanchez-Carron, D.Campopiano, G.Grogan. Structure of N-Acylamino Acid Racemase Mutants in Complex with Substrates To Be Published.
Page generated: Sun Sep 29 04:19:05 2024

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