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Magnesium in PDB 5fju: N-Acyl Amino Acid Racemase From Amycolatopsis Sp. Ts-1-60: Q26A M50I G291D F323Y Mutant in Complex with N-Acetyl Phenylalanine

Enzymatic activity of N-Acyl Amino Acid Racemase From Amycolatopsis Sp. Ts-1-60: Q26A M50I G291D F323Y Mutant in Complex with N-Acetyl Phenylalanine

All present enzymatic activity of N-Acyl Amino Acid Racemase From Amycolatopsis Sp. Ts-1-60: Q26A M50I G291D F323Y Mutant in Complex with N-Acetyl Phenylalanine:
4.2.1.113;

Protein crystallography data

The structure of N-Acyl Amino Acid Racemase From Amycolatopsis Sp. Ts-1-60: Q26A M50I G291D F323Y Mutant in Complex with N-Acetyl Phenylalanine, PDB code: 5fju 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) 107.35 / 2.52
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 216.900, 216.900, 261.630, 90.00, 90.00, 120.00
R / Rfree (%) 15.6 / 19

Magnesium Binding Sites:

The binding sites of Magnesium atom in the N-Acyl Amino Acid Racemase From Amycolatopsis Sp. Ts-1-60: Q26A M50I G291D F323Y Mutant in Complex with N-Acetyl Phenylalanine (pdb code 5fju). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the N-Acyl Amino Acid Racemase From Amycolatopsis Sp. Ts-1-60: Q26A M50I G291D F323Y Mutant in Complex with N-Acetyl Phenylalanine, PDB code: 5fju:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 5fju

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Magnesium binding site 1 out of 4 in the N-Acyl Amino Acid Racemase From Amycolatopsis Sp. Ts-1-60: Q26A M50I G291D F323Y Mutant in Complex with N-Acetyl Phenylalanine


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: Q26A M50I G291D F323Y Mutant in Complex with N-Acetyl Phenylalanine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1369

b:50.1
occ:1.00
 OD2 A:ASP239 2.3 41.6 1.0
OE2 A:GLU214 2.4 54.3 1.0
OD2 A:ASP189 2.5 42.2 1.0
OXT A:5CR1370 2.5 49.4 1.0
O A:5CR1370 3.0 56.9 1.0
CD A:GLU214 3.0 47.6 1.0
OD1 A:ASP189 3.1 45.6 1.0
CG A:ASP189 3.1 37.8 1.0
C A:5CR1370 3.1 51.8 1.0
CG A:ASP239 3.3 35.6 1.0
ND2 A:ASN191 3.4 43.8 1.0
CG A:GLU214 3.7 38.4 1.0
CB A:ASP239 3.7 32.5 1.0
OE1 A:GLU214 3.8 46.8 1.0
OE1 A:GLU240 3.8 41.3 1.0
NZ A:LYS263 4.0 62.8 1.0
CG A:ASN191 4.2 44.1 1.0
NZ A:LYS163 4.3 45.8 1.0
NZ A:LYS161 4.3 42.4 1.0
OD1 A:ASP239 4.4 40.7 1.0
OD1 A:ASN191 4.5 50.5 1.0
CB A:ASP189 4.6 34.8 1.0
CD A:GLU240 4.6 42.4 1.0
CA A:5CR1370 4.7 46.4 1.0
OE2 A:GLU240 4.7 44.0 1.0
CB A:GLU214 4.7 34.9 1.0
ND2 A:ASN261 4.7 51.9 1.0
CE2 A:TYR55 5.0 43.4 1.0

Magnesium binding site 2 out of 4 in 5fju

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Magnesium binding site 2 out of 4 in the N-Acyl Amino Acid Racemase From Amycolatopsis Sp. Ts-1-60: Q26A M50I G291D F323Y Mutant in Complex with N-Acetyl Phenylalanine


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: Q26A M50I G291D F323Y Mutant in Complex with N-Acetyl Phenylalanine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1368

b:56.0
occ:1.00
 OD2 B:ASP239 2.5 47.5 1.0
OD2 B:ASP189 2.7 37.4 1.0
OXT B:5CR1369 2.7 57.2 1.0
OD1 B:ASP189 2.8 40.0 1.0
OE2 B:GLU214 2.8 47.5 1.0
CG B:ASP189 3.1 35.7 1.0
ND2 B:ASN191 3.1 47.0 1.0
OE1 B:GLU240 3.3 43.9 1.0
CD B:GLU214 3.3 50.6 1.0
CG B:ASP239 3.4 50.1 1.0
CB B:ASP239 3.6 40.0 1.0
CG B:GLU214 3.6 44.6 1.0
C B:5CR1369 3.7 53.8 1.0
CG B:ASN191 3.9 48.3 1.0
O B:5CR1369 3.9 59.7 1.0
CD B:GLU240 4.1 47.4 1.0
OE2 B:GLU240 4.1 54.6 1.0
OE1 B:GLU214 4.2 51.9 1.0
OD1 B:ASN191 4.3 46.9 1.0
CB B:GLN215 4.5 33.5 1.0
CA B:ASN191 4.5 38.1 1.0
NZ B:LYS163 4.5 43.6 1.0
OD1 B:ASP239 4.5 45.6 1.0
N B:ASN191 4.5 35.7 1.0
NZ B:LYS263 4.5 65.4 1.0
CB B:ASP189 4.6 32.6 1.0
CB B:GLU214 4.6 43.5 1.0
CB B:ASN191 4.8 41.0 1.0
NZ B:LYS161 4.9 49.4 1.0
CE2 B:TYR55 4.9 45.4 1.0
O B:GLU214 5.0 37.3 1.0

Magnesium binding site 3 out of 4 in 5fju

Go back to Magnesium Binding Sites List in 5fju
Magnesium binding site 3 out of 4 in the N-Acyl Amino Acid Racemase From Amycolatopsis Sp. Ts-1-60: Q26A M50I G291D F323Y Mutant in Complex with N-Acetyl Phenylalanine


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of N-Acyl Amino Acid Racemase From Amycolatopsis Sp. Ts-1-60: Q26A M50I G291D F323Y Mutant in Complex with N-Acetyl Phenylalanine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg1368

b:51.8
occ:1.00
 OD2 C:ASP239 2.4 56.9 1.0
OXT C:5CR1370 2.6 56.6 1.0
OD2 C:ASP189 2.7 50.7 1.0
OE2 C:GLU214 2.7 44.2 1.0
OD1 C:ASP189 2.9 54.2 1.0
CG C:ASP189 3.1 49.0 1.0
ND2 C:ASN191 3.2 54.7 1.0
CD C:GLU214 3.2 51.5 1.0
OE1 C:GLU240 3.3 41.6 1.0
CG C:ASP239 3.3 41.0 1.0
CB C:ASP239 3.5 40.8 1.0
CG C:GLU214 3.6 42.1 1.0
C C:5CR1370 3.7 52.5 1.0
CG C:ASN191 4.0 52.0 1.0
O C:5CR1370 4.0 69.9 1.0
OE1 C:GLU214 4.1 49.4 1.0
CD C:GLU240 4.1 41.6 1.0
OE2 C:GLU240 4.2 41.8 1.0
OD1 C:ASP239 4.4 41.8 1.0
OD1 C:ASN191 4.4 48.0 1.0
NZ C:LYS263 4.5 55.5 1.0
CB C:GLN215 4.5 38.8 1.0
CB C:GLU214 4.6 36.7 1.0
NZ C:LYS163 4.6 52.7 1.0
CB C:ASP189 4.6 47.8 1.0
CA C:ASN191 4.6 44.7 1.0
N C:ASN191 4.6 40.1 1.0
NZ C:LYS161 4.9 52.0 1.0
CB C:ASN191 4.9 49.2 1.0
CE2 C:TYR55 5.0 49.9 1.0

Magnesium binding site 4 out of 4 in 5fju

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Magnesium binding site 4 out of 4 in the N-Acyl Amino Acid Racemase From Amycolatopsis Sp. Ts-1-60: Q26A M50I G291D F323Y Mutant in Complex with N-Acetyl Phenylalanine


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of N-Acyl Amino Acid Racemase From Amycolatopsis Sp. Ts-1-60: Q26A M50I G291D F323Y Mutant in Complex with N-Acetyl Phenylalanine within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg1368

b:51.7
occ:1.00
 O D:HOH2063 2.2 36.9 1.0
OD1 D:ASP189 2.6 44.8 1.0
OD2 D:ASP239 2.8 47.6 1.0
OE1 D:GLU240 2.9 38.2 1.0
ND2 D:ASN191 3.0 43.1 1.0
OD2 D:ASP189 3.0 46.5 1.0
CG D:ASP189 3.2 40.5 1.0
OE2 D:GLU214 3.3 53.2 1.0
CG D:ASP239 3.6 47.0 1.0
OXT D:5CR1370 3.6 45.4 1.0
CD D:GLU214 3.6 50.8 1.0
CB D:ASP239 3.7 43.6 1.0
CG D:GLU214 3.7 43.7 1.0
CG D:ASN191 3.7 43.0 1.0
CD D:GLU240 3.7 42.5 1.0
OE2 D:GLU240 3.8 43.0 1.0
CB D:GLN215 3.9 38.9 1.0
CA D:ASN191 4.0 37.6 1.0
N D:ASN191 4.0 34.0 1.0
OD1 D:ASN191 4.3 48.1 1.0
CB D:ASN191 4.5 43.3 1.0
O D:GLU214 4.5 33.9 1.0
OE1 D:GLU214 4.5 49.0 1.0
CB D:GLU214 4.5 40.8 1.0
C D:5CR1370 4.6 53.4 1.0
CB D:ASP189 4.6 40.7 1.0
C D:GLU214 4.6 35.6 1.0
CG D:GLN215 4.7 36.0 1.0
OD1 D:ASP239 4.7 46.9 1.0
O D:5CR1370 4.9 57.7 1.0
NZ D:LYS163 4.9 47.3 1.0
N D:GLN215 4.9 39.5 1.0
CA D:GLN215 5.0 37.8 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 04:19:06 2024

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