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Magnesium in PDB 4a6g: N-Acyl Amino Acid Racemase From Amycalotopsis Sp. Ts-1-60: G291D-F323Y Mutant in Complex with N-Acetyl Methionine

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

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

Protein crystallography data

The structure of N-Acyl Amino Acid Racemase From Amycalotopsis Sp. Ts-1-60: G291D-F323Y Mutant in Complex with N-Acetyl Methionine, PDB code: 4a6g was solved by S.Baxter, S.Royer, G.Grogan, K.E.Holt-Tiffin, I.N.Taylor, I.G.Fotheringham, D.J.Campopiano, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 88.31 / 2.71
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 216.710, 216.710, 261.100, 90.00, 90.00, 120.00
R / Rfree (%) 15.535 / 21.012

Magnesium Binding Sites:

The binding sites of Magnesium atom in the N-Acyl Amino Acid Racemase From Amycalotopsis Sp. Ts-1-60: G291D-F323Y Mutant in Complex with N-Acetyl Methionine (pdb code 4a6g). 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 Amycalotopsis Sp. Ts-1-60: G291D-F323Y Mutant in Complex with N-Acetyl Methionine, PDB code: 4a6g:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 4a6g

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


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 Amycalotopsis Sp. Ts-1-60: G291D-F323Y Mutant in Complex with N-Acetyl Methionine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1370

b:73.9
occ:1.00
 OE2 A:GLU214 2.3 59.0 1.0
O A:HOH2065 2.4 43.0 1.0
O A:AME1369 2.4 68.0 1.0
OD2 A:ASP189 2.5 42.1 1.0
OD2 A:ASP239 2.5 43.6 1.0
OXT A:AME1369 2.7 50.5 1.0
C A:AME1369 2.9 56.9 1.0
CD A:GLU214 3.1 58.1 1.0
CG A:ASP189 3.3 44.1 1.0
OD1 A:ASP189 3.5 45.6 1.0
CG A:ASP239 3.6 40.5 1.0
OE1 A:GLU214 3.7 58.0 1.0
OD1 A:ASN191 3.8 64.8 1.0
NZ A:LYS161 3.9 35.5 1.0
NZ A:LYS163 3.9 49.4 1.0
CB A:ASP239 4.0 35.7 1.0
CG A:GLU214 4.0 47.2 1.0
NZ A:LYS263 4.2 32.1 1.0
ND2 A:ASN261 4.4 44.5 1.0
OE1 A:GLU240 4.4 46.6 1.0
O A:HOH2061 4.4 53.1 1.0
CG A:ASN191 4.4 57.7 1.0
CA A:AME1369 4.4 61.5 1.0
ND2 A:ASN191 4.5 51.7 1.0
CB A:ASP189 4.6 38.3 1.0
OD1 A:ASP239 4.7 47.4 1.0
CE A:LYS161 4.7 34.8 1.0
N A:AME1369 4.7 64.2 1.0
CE A:LYS263 4.9 31.1 1.0
CB A:GLU214 5.0 38.6 1.0

Magnesium binding site 2 out of 4 in 4a6g

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


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 Amycalotopsis Sp. Ts-1-60: G291D-F323Y Mutant in Complex with N-Acetyl Methionine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1369

b:63.8
occ:1.00
 OE2 B:GLU214 2.0 49.6 1.0
OD2 B:ASP239 2.4 56.9 1.0
OD2 B:ASP189 2.4 51.1 1.0
O B:HOH2044 2.5 41.7 1.0
OXT B:AME1368 2.7 60.2 1.0
O B:AME1368 2.8 62.1 1.0
CD B:GLU214 2.8 54.6 1.0
C B:AME1368 3.1 58.5 1.0
CG B:ASP189 3.2 50.5 1.0
CG B:ASP239 3.3 52.8 1.0
OD1 B:ASP189 3.5 48.1 1.0
CB B:ASP239 3.6 42.5 1.0
OE1 B:GLU214 3.6 52.5 1.0
CG B:GLU214 3.6 51.5 1.0
OD1 B:ASN191 3.9 56.9 1.0
NZ B:LYS161 4.0 43.6 1.0
OE1 B:GLU240 4.2 44.1 1.0
NZ B:LYS263 4.2 46.2 1.0
O B:HOH2041 4.4 52.9 1.0
ND2 B:ASN261 4.4 51.2 1.0
NZ B:LYS163 4.4 42.7 1.0
OD1 B:ASP239 4.4 52.6 1.0
CB B:ASP189 4.6 40.1 1.0
CG B:ASN191 4.6 49.2 1.0
CE B:LYS263 4.6 39.2 1.0
CA B:AME1368 4.6 57.1 1.0
CE B:LYS161 4.7 44.3 1.0
ND2 B:ASN191 4.7 38.5 1.0
CB B:GLU214 4.8 46.0 1.0
CD B:GLU240 5.0 42.1 1.0

Magnesium binding site 3 out of 4 in 4a6g

Go back to Magnesium Binding Sites List in 4a6g
Magnesium binding site 3 out of 4 in the N-Acyl Amino Acid Racemase From Amycalotopsis Sp. Ts-1-60: G291D-F323Y Mutant in Complex with N-Acetyl Methionine


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 Amycalotopsis Sp. Ts-1-60: G291D-F323Y Mutant in Complex with N-Acetyl Methionine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg1369

b:55.9
occ:1.00
 O C:HOH2031 1.8 53.5 1.0
OD2 C:ASP239 2.3 53.4 1.0
O C:AME1368 2.7 62.7 1.0
OE2 C:GLU214 2.8 52.2 1.0
OD2 C:ASP189 2.9 43.4 1.0
OXT C:AME1368 3.0 76.0 1.0
C C:AME1368 3.3 67.3 1.0
CG C:ASP239 3.3 47.1 1.0
OD1 C:ASN191 3.3 52.5 1.0
CD C:GLU214 3.4 54.7 1.0
OD1 C:ASP189 3.4 55.1 1.0
OE1 C:GLU240 3.4 53.1 1.0
CG C:ASP189 3.4 49.5 1.0
CB C:ASP239 3.6 42.1 1.0
CG C:GLU214 3.9 46.8 1.0
CG C:ASN191 4.1 51.1 1.0
NZ C:LYS263 4.1 40.6 1.0
OE1 C:GLU214 4.2 65.8 1.0
NZ C:LYS163 4.3 49.6 1.0
OD1 C:ASP239 4.4 45.1 1.0
CD C:GLU240 4.4 47.5 1.0
ND2 C:ASN191 4.6 51.8 1.0
OE2 C:GLU240 4.6 44.1 1.0
NZ C:LYS161 4.6 48.7 1.0
CA C:AME1368 4.7 64.1 1.0
ND2 C:ASN261 4.7 40.8 1.0
CB C:ASP189 4.8 45.8 1.0
CE1 C:TYR55 4.8 50.1 1.0
CB C:GLU214 4.9 41.9 1.0
CA C:ASN191 4.9 51.0 1.0

Magnesium binding site 4 out of 4 in 4a6g

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


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 Amycalotopsis Sp. Ts-1-60: G291D-F323Y Mutant in Complex with N-Acetyl Methionine within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg1369

b:62.8
occ:1.00
 O D:HOH2035 2.1 52.5 1.0
OD2 D:ASP189 2.4 51.8 1.0
OD2 D:ASP239 2.4 47.2 1.0
OE2 D:GLU214 2.6 47.1 1.0
O D:AME1368 2.6 72.7 1.0
OXT D:AME1368 3.0 64.7 1.0
C D:AME1368 3.2 68.9 1.0
CG D:ASP189 3.2 48.7 1.0
CD D:GLU214 3.2 49.3 1.0
OD1 D:ASP189 3.4 47.5 1.0
OD1 D:ASN191 3.4 50.0 1.0
CG D:ASP239 3.5 49.3 1.0
NZ D:LYS263 3.6 43.9 1.0
CG D:GLU214 3.8 43.1 1.0
OE2 D:GLU240 3.9 52.9 1.0
CB D:ASP239 3.9 45.0 1.0
OE1 D:GLU214 4.0 44.0 1.0
CG D:ASN191 4.0 50.8 1.0
NZ D:LYS163 4.1 47.8 1.0
NZ D:LYS161 4.2 47.0 1.0
ND2 D:ASN191 4.2 50.0 1.0
OD1 D:ASP239 4.5 44.9 1.0
CB D:ASP189 4.6 44.0 1.0
CA D:AME1368 4.7 64.7 1.0
ND2 D:ASN261 4.7 54.0 1.0
CE D:LYS161 4.8 43.4 1.0
CE D:LYS263 4.9 46.8 1.0
O D:HOH2030 4.9 41.0 1.0
CD D:GLU240 4.9 54.0 1.0
CB D:GLU214 5.0 36.9 1.0

Reference:

S.Baxter, S.Royer, G.Grogan, F.Brown, K.E.Holt-Tiffin, I.N.Taylor, I.G.Fotheringham, D.J.Campopiano. An Improved Racemase/Acylase Biotransformation For the Preparation of Enantiomerically Pure Amino Acids. J.Am.Chem.Soc. V. 134 19310 2012.
ISSN: ISSN 0002-7863
PubMed: 23130969
DOI: 10.1021/JA305438Y
Page generated: Mon Dec 14 09:06:29 2020

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