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Magnesium in PDB 2jcb: The Crystal Structure of 5-Formyl-Tetrahydrofolate Cycloligase From Bacillus Anthracis (BA4489)

Enzymatic activity of The Crystal Structure of 5-Formyl-Tetrahydrofolate Cycloligase From Bacillus Anthracis (BA4489)

All present enzymatic activity of The Crystal Structure of 5-Formyl-Tetrahydrofolate Cycloligase From Bacillus Anthracis (BA4489):
6.3.3.2;

Protein crystallography data

The structure of The Crystal Structure of 5-Formyl-Tetrahydrofolate Cycloligase From Bacillus Anthracis (BA4489), PDB code: 2jcb was solved by C.Meier, L.G.Carter, G.Winter, R.J.Owens, D.I.Stuart, R.M.Esnouf, Oxford Protein Production Facility (Oppf), Structural Proteomics Ineurope (Spine), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 18.69 / 1.6
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 37.152, 45.499, 66.999, 74.92, 78.01, 70.14
R / Rfree (%) 18.9 / 23.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The Crystal Structure of 5-Formyl-Tetrahydrofolate Cycloligase From Bacillus Anthracis (BA4489) (pdb code 2jcb). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the The Crystal Structure of 5-Formyl-Tetrahydrofolate Cycloligase From Bacillus Anthracis (BA4489), PDB code: 2jcb:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 2jcb

Go back to Magnesium Binding Sites List in 2jcb
Magnesium binding site 1 out of 2 in the The Crystal Structure of 5-Formyl-Tetrahydrofolate Cycloligase From Bacillus Anthracis (BA4489)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Crystal Structure of 5-Formyl-Tetrahydrofolate Cycloligase From Bacillus Anthracis (BA4489) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1192

b:20.9
occ:1.00
OD2 A:ASP144 1.9 29.0 1.0
O1A A:ADP1190 2.1 34.6 1.0
O A:HOH2157 2.1 22.4 1.0
OD1 A:ASP173 2.1 29.2 1.0
O3B A:ADP1190 2.1 33.7 1.0
O A:HOH2198 2.3 24.5 1.0
CG A:ASP144 3.0 25.9 1.0
PB A:ADP1190 3.2 32.7 1.0
CG A:ASP173 3.3 29.1 1.0
PA A:ADP1190 3.3 33.1 1.0
OD1 A:ASP144 3.4 30.2 1.0
O3A A:ADP1190 3.6 33.6 1.0
NZ A:LYS5 3.7 31.4 1.0
O2B A:ADP1190 3.7 34.5 1.0
OD2 A:ASP173 4.0 29.6 1.0
O A:HOH2150 4.0 39.3 1.0
O A:HOH2200 4.1 19.8 1.0
O5' A:ADP1190 4.1 34.2 1.0
CB A:ASP173 4.2 28.2 1.0
CE1 A:PHE172 4.3 35.6 1.0
CA A:ASP173 4.3 28.8 1.0
CB A:ASP144 4.3 26.5 1.0
O A:ARG135 4.3 29.7 1.0
O2A A:ADP1190 4.5 31.8 1.0
O1B A:ADP1190 4.5 31.0 1.0
CD1 A:PHE172 4.5 35.8 1.0
CE A:LYS5 4.9 30.5 1.0
NH2 A:ARG135 5.0 32.8 1.0

Magnesium binding site 2 out of 2 in 2jcb

Go back to Magnesium Binding Sites List in 2jcb
Magnesium binding site 2 out of 2 in the The Crystal Structure of 5-Formyl-Tetrahydrofolate Cycloligase From Bacillus Anthracis (BA4489)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of The Crystal Structure of 5-Formyl-Tetrahydrofolate Cycloligase From Bacillus Anthracis (BA4489) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1191

b:28.6
occ:1.00
O B:HOH2120 1.9 27.6 1.0
O2A B:ADP1189 2.1 26.6 1.0
OD2 B:ASP144 2.1 26.9 1.0
O1B B:ADP1189 2.2 27.4 1.0
OD1 B:ASP173 2.2 29.7 1.0
O B:HOH2092 2.3 27.8 1.0
PB B:ADP1189 3.2 27.2 1.0
CG B:ASP144 3.2 26.4 1.0
PA B:ADP1189 3.3 27.0 1.0
CG B:ASP173 3.4 28.9 1.0
O3A B:ADP1189 3.5 27.7 1.0
OD1 B:ASP144 3.6 26.0 1.0
O2B B:ADP1189 3.6 25.0 1.0
NZ B:LYS5 3.8 29.1 1.0
O5' B:ADP1189 4.1 26.5 1.0
O B:ARG135 4.1 26.5 1.0
CE1 B:PHE172 4.1 32.3 1.0
O B:HOH2121 4.1 26.5 1.0
OD2 B:ASP173 4.2 28.7 1.0
CB B:ASP173 4.3 28.2 1.0
CA B:ASP173 4.4 28.6 1.0
CE B:LYS5 4.4 30.4 1.0
CB B:ASP144 4.5 26.8 1.0
O1A B:ADP1189 4.5 23.0 1.0
O3B B:ADP1189 4.5 30.8 1.0
CD1 B:PHE172 4.6 31.7 1.0

Reference:

C.Meier, L.G.Carter, G.Winter, R.J.Owens, D.I.Stuart, R.M.Esnouf. Structure of 5-Formyltetrahydrofolate Cyclo-Ligase From Bacillus Anthracis (BA4489). Acta Crystallogr.,Sect.F V. 63 168 2007.
ISSN: ISSN 1744-3091
PubMed: 17329806
DOI: 10.1107/S1744309107007221
Page generated: Mon Dec 14 07:29:18 2020

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