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Manganese in PDB 4ipj: Crystal Structure of R314K N-Acetyl Neuraminic Acid Synthase From Neiserria Meningitidis with Malate Bound

Enzymatic activity of Crystal Structure of R314K N-Acetyl Neuraminic Acid Synthase From Neiserria Meningitidis with Malate Bound

All present enzymatic activity of Crystal Structure of R314K N-Acetyl Neuraminic Acid Synthase From Neiserria Meningitidis with Malate Bound:
2.5.1.56;

Protein crystallography data

The structure of Crystal Structure of R314K N-Acetyl Neuraminic Acid Synthase From Neiserria Meningitidis with Malate Bound, PDB code: 4ipj was solved by D.D.A.Joseph, W.Jiao, E.J.Parker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.15 / 2.15
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 58.230, 76.050, 77.670, 90.00, 90.00, 90.00
R / Rfree (%) 17.4 / 24.2

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of R314K N-Acetyl Neuraminic Acid Synthase From Neiserria Meningitidis with Malate Bound (pdb code 4ipj). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Crystal Structure of R314K N-Acetyl Neuraminic Acid Synthase From Neiserria Meningitidis with Malate Bound, PDB code: 4ipj:

Manganese binding site 1 out of 1 in 4ipj

Go back to Manganese Binding Sites List in 4ipj
Manganese binding site 1 out of 1 in the Crystal Structure of R314K N-Acetyl Neuraminic Acid Synthase From Neiserria Meningitidis with Malate Bound


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of R314K N-Acetyl Neuraminic Acid Synthase From Neiserria Meningitidis with Malate Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn401

b:21.2
occ:1.00
 O A:HOH517 1.7 14.0 1.0
NE2 A:HIS215 2.1 8.6 1.0
O1B A:LMR402 2.2 40.4 1.0
NE2 A:HIS236 2.3 14.6 1.0
O2 A:LMR402 2.4 33.1 1.0
OH A:TYR186 2.6 24.4 0.5
C1 A:LMR402 2.8 39.4 1.0
C2 A:LMR402 3.1 37.3 1.0
CD2 A:HIS215 3.1 9.9 1.0
CE1 A:HIS215 3.1 10.3 1.0
CD2 A:HIS236 3.2 14.6 1.0
CE1 A:HIS236 3.4 18.2 1.0
CZ A:TYR186 3.6 25.5 0.5
OE1 A:GLU25 3.6 26.0 1.0
O1A A:LMR402 3.7 43.6 1.0
O A:HOH616 3.7 23.5 1.0
C3 A:LMR402 3.8 36.6 1.0
CE2 A:TYR186 4.1 18.3 0.5
ND1 A:HIS215 4.2 10.0 1.0
CE1 A:TYR186 4.2 25.1 0.5
CG A:HIS215 4.3 10.8 1.0
OH A:TYR186 4.4 12.8 0.5
CG A:HIS236 4.4 11.7 1.0
ND1 A:HIS236 4.5 16.3 1.0
CD A:GLU25 4.5 19.3 1.0
CE2 A:TYR186 4.5 25.4 0.5
O A:HOH687 4.5 31.4 1.0
OE2 A:GLU25 4.6 19.4 1.0
O A:HOH611 4.6 18.2 1.0
O A:HOH518 4.7 16.5 1.0
OG A:SER213 4.8 11.5 1.0
CZ A:TYR186 4.8 17.2 0.5
C4 A:LMR402 4.9 36.2 1.0

Reference:

D.D.Joseph, W.Jiao, E.J.Parker. ARG314 Is Essential For Catalysis By N-Acetyl Neuraminic Acid Synthase From Neisseria Meningitidis. Biochemistry V. 52 2609 2013.
ISSN: ISSN 0006-2960
PubMed: 23534460
DOI: 10.1021/BI400062C
Page generated: Sat Oct 5 19:51:56 2024

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