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Manganese in PDB 3qcz: Crystal Structure of Bifunctional Folylpolyglutamate Synthase/Dihydrofolate Synthase with Mn, Amppnp and L-Glutamate Bound

Enzymatic activity of Crystal Structure of Bifunctional Folylpolyglutamate Synthase/Dihydrofolate Synthase with Mn, Amppnp and L-Glutamate Bound

All present enzymatic activity of Crystal Structure of Bifunctional Folylpolyglutamate Synthase/Dihydrofolate Synthase with Mn, Amppnp and L-Glutamate Bound:
6.3.2.17;

Protein crystallography data

The structure of Crystal Structure of Bifunctional Folylpolyglutamate Synthase/Dihydrofolate Synthase with Mn, Amppnp and L-Glutamate Bound, PDB code: 3qcz was solved by B.Nocek, M.Makowska-Grzyska, N.Maltseva, W.Anderson, A.Joachimiak, Centerfor Structural Genomics Of Infectious Diseases (Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 62.861, 83.237, 126.990, 90.00, 90.00, 90.00
R / Rfree (%) 17.1 / 19.9

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Bifunctional Folylpolyglutamate Synthase/Dihydrofolate Synthase with Mn, Amppnp and L-Glutamate Bound (pdb code 3qcz). 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 Bifunctional Folylpolyglutamate Synthase/Dihydrofolate Synthase with Mn, Amppnp and L-Glutamate Bound, PDB code: 3qcz:

Manganese binding site 1 out of 1 in 3qcz

Go back to Manganese Binding Sites List in 3qcz
Manganese binding site 1 out of 1 in the Crystal Structure of Bifunctional Folylpolyglutamate Synthase/Dihydrofolate Synthase with Mn, Amppnp and L-Glutamate 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 Bifunctional Folylpolyglutamate Synthase/Dihydrofolate Synthase with Mn, Amppnp and L-Glutamate Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn601

b:31.0
occ:1.00
 O1G A:ANP501 2.0 30.9 1.0
OE2 A:GLU146 2.0 27.8 1.0
O1B A:ANP501 2.1 31.7 1.0
O A:SER83 2.2 29.2 1.0
O A:HOH436 2.3 27.1 1.0
O A:HOH437 2.3 30.1 1.0
CD A:GLU146 3.0 27.6 1.0
PG A:ANP501 3.3 35.6 1.0
OE1 A:GLU146 3.3 29.9 1.0
PB A:ANP501 3.3 26.0 1.0
C A:SER83 3.4 27.9 1.0
N3B A:ANP501 3.5 29.3 1.0
CD A:PRO84 3.9 32.5 1.0
O A:HOH494 4.0 31.4 1.0
O A:HOH481 4.0 33.4 1.0
N A:PRO84 4.1 31.5 1.0
O2B A:ANP501 4.2 24.4 1.0
O3G A:ANP501 4.2 35.7 1.0
N A:GLY61 4.3 24.2 1.0
NH1 A:ARG301 4.3 31.5 1.0
O2G A:ANP501 4.3 37.4 1.0
CG A:GLU146 4.4 27.1 1.0
O A:HOH531 4.5 40.2 1.0
CA A:GLY61 4.5 24.5 1.0
O2A A:ANP501 4.5 28.1 1.0
CE A:LYS60 4.6 25.3 1.0
N A:SER83 4.6 28.1 1.0
CA A:SER83 4.6 28.8 1.0
O3A A:ANP501 4.6 30.1 1.0
CB A:LYS60 4.8 25.6 1.0
NZ A:LYS60 4.8 24.3 1.0

Reference:

B.Nocek, M.Makowska-Grzyska, N.Maltseva, W.Anderson, A.Joachimiak, Center For Structural Genomics Of Infectious Diseases(Csgid). Crystal Structure of Bifunctional Folylpolyglutamate Synthase/Dihydrofolate Synthase with Mn, Amppnp and L-Glutamate Bound To Be Published.
Page generated: Tue Dec 15 04:14:15 2020

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