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Magnesium in PDB 3ahh: H142A Mutant of Phosphoketolase From Bifidobacterium Breve Complexed with Acetyl Thiamine Diphosphate

Enzymatic activity of H142A Mutant of Phosphoketolase From Bifidobacterium Breve Complexed with Acetyl Thiamine Diphosphate

All present enzymatic activity of H142A Mutant of Phosphoketolase From Bifidobacterium Breve Complexed with Acetyl Thiamine Diphosphate:
4.1.2.22;

Protein crystallography data

The structure of H142A Mutant of Phosphoketolase From Bifidobacterium Breve Complexed with Acetyl Thiamine Diphosphate, PDB code: 3ahh was solved by R.Suzuki, T.Katayama, B.-J.Kim, T.Wakagi, H.Shoun, H.Ashida, K.Yamamoto, S.Fushinobu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.15 / 2.10
Space group I 4 2 2
Cell size a, b, c (Å), α, β, γ (°) 174.606, 174.606, 163.644, 90.00, 90.00, 90.00
R / Rfree (%) 15.8 / 19.6

Other elements in 3ahh:

The structure of H142A Mutant of Phosphoketolase From Bifidobacterium Breve Complexed with Acetyl Thiamine Diphosphate also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the H142A Mutant of Phosphoketolase From Bifidobacterium Breve Complexed with Acetyl Thiamine Diphosphate (pdb code 3ahh). 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 H142A Mutant of Phosphoketolase From Bifidobacterium Breve Complexed with Acetyl Thiamine Diphosphate, PDB code: 3ahh:

Magnesium binding site 1 out of 1 in 3ahh

Go back to Magnesium Binding Sites List in 3ahh
Magnesium binding site 1 out of 1 in the H142A Mutant of Phosphoketolase From Bifidobacterium Breve Complexed with Acetyl Thiamine Diphosphate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of H142A Mutant of Phosphoketolase From Bifidobacterium Breve Complexed with Acetyl Thiamine Diphosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg826

b:16.6
occ:1.00
 O12 A:HTL827 2.1 16.2 1.0
OD1 A:ASP182 2.1 16.8 1.0
O21 A:HTL827 2.1 17.1 1.0
OD1 A:ASN215 2.2 14.7 1.0
O A:TYR217 2.2 16.3 1.0
O A:HOH1251 2.2 14.1 1.0
CG A:ASN215 3.1 16.8 1.0
P2 A:HTL827 3.2 17.0 1.0
P1 A:HTL827 3.2 17.2 1.0
CG A:ASP182 3.3 15.2 1.0
C A:TYR217 3.4 17.1 1.0
ND2 A:ASN215 3.4 14.6 1.0
O11 A:HTL827 3.5 15.0 1.0
O22 A:HTL827 3.6 14.8 1.0
OD2 A:ASP182 3.9 15.1 1.0
N A:ASP182 3.9 15.5 1.0
N A:TYR217 4.0 15.4 1.0
O5G A:HTL827 4.1 18.3 1.0
N A:GLY183 4.1 16.0 1.0
O A:HIS213 4.1 15.1 1.0
NZ A:LYS300 4.3 15.3 1.0
N A:LYS218 4.3 17.8 1.0
CA A:TYR217 4.3 16.8 1.0
O13 A:HTL827 4.3 15.2 1.0
CG2 A:THR223 4.4 12.3 1.0
CA A:LYS218 4.4 14.6 1.0
CB A:ASP182 4.4 13.3 1.0
CA A:ASP182 4.5 15.3 1.0
CB A:ASN215 4.5 15.4 1.0
N A:ASN215 4.5 16.8 1.0
O23 A:HTL827 4.5 20.2 1.0
CD A:LYS300 4.6 12.6 1.0
C A:ASP182 4.7 14.9 1.0
N A:GLY216 4.7 15.9 1.0
CA A:ASN215 4.8 16.4 1.0
C A:ASN215 4.9 14.8 1.0
C A:GLY181 4.9 15.4 1.0
CE A:LYS300 5.0 16.0 1.0

Reference:

R.Suzuki, T.Katayama, B.-J.Kim, T.Wakagi, H.Shoun, H.Ashida, K.Yamamoto, S.Fushinobu. Crystal Structures of Phosphoketolase: Thiamine Diphosphate-Dependent Dehydration Mechanism J.Biol.Chem. V. 285 34279 2010.
ISSN: ISSN 0021-9258
PubMed: 20739284
DOI: 10.1074/JBC.M110.156281
Page generated: Wed Aug 14 08:36:21 2024

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