Atomistry » Magnesium » PDB 5fjo-5fuk » 5fju
Atomistry »
  Magnesium »
    PDB 5fjo-5fuk »
      5fju »

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

Go back to Magnesium Binding Sites List in 5fju
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

Go back to Magnesium Binding Sites List in 5fju
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

Go back to Magnesium Binding Sites List in 5fju
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

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy