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Potassium in PDB 2fca: The Structure of Bstrmb

Enzymatic activity of The Structure of Bstrmb

All present enzymatic activity of The Structure of Bstrmb:
2.1.1.33;

Protein crystallography data

The structure of The Structure of Bstrmb, PDB code: 2fca was solved by I.Zegers, F.Van Vliet, J.Bujnicki, J.Kosinski, D.Gigot, L.Droogmans, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.10
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 178.830, 178.830, 41.950, 90.00, 90.00, 120.00
R / Rfree (%) 20.2 / 23.3

Potassium Binding Sites:

The binding sites of Potassium atom in the The Structure of Bstrmb (pdb code 2fca). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 3 binding sites of Potassium where determined in the The Structure of Bstrmb, PDB code: 2fca:
Jump to Potassium binding site number: 1; 2; 3;

Potassium binding site 1 out of 3 in 2fca

Go back to Potassium Binding Sites List in 2fca
Potassium binding site 1 out of 3 in the The Structure of Bstrmb


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of The Structure of Bstrmb within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K250

b:38.0
occ:1.00
O A:ASN115 2.5 32.9 1.0
O A:GLY46 2.5 32.5 1.0
O A:HOH578 2.7 49.8 1.0
O A:HOH257 2.8 23.5 1.0
O A:HOH272 3.1 35.6 1.0
O A:HOH486 3.2 46.9 1.0
O A:HOH500 3.5 53.6 1.0
C A:GLY46 3.5 32.5 1.0
C A:ASN115 3.7 32.2 1.0
CA A:GLY46 4.0 31.2 1.0
O A:VAL45 4.2 28.2 1.0
O A:HOH307 4.2 31.1 1.0
O A:PHE116 4.4 32.5 1.0
CA A:ASN115 4.4 31.6 1.0
C A:PHE116 4.4 32.8 1.0
N A:ASN115 4.4 30.4 1.0
CB A:ASN115 4.5 32.0 1.0
N A:SER117 4.6 32.7 1.0
OE1 A:GLU44 4.6 27.9 1.0
N A:PHE116 4.7 32.4 1.0
N A:THR47 4.7 33.6 1.0
O A:HOH273 4.8 34.8 1.0
CA A:SER117 4.8 33.4 1.0
O A:HOH570 4.8 52.3 1.0
N A:GLY46 5.0 29.4 1.0
OG A:SER117 5.0 31.0 1.0
C A:VAL45 5.0 28.9 1.0

Potassium binding site 2 out of 3 in 2fca

Go back to Potassium Binding Sites List in 2fca
Potassium binding site 2 out of 3 in the The Structure of Bstrmb


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of The Structure of Bstrmb within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K252

b:38.2
occ:1.00
OG B:SER167 3.0 27.8 1.0
OG A:SER167 3.1 31.7 1.0
O B:HOH356 3.2 34.0 1.0
O B:HOH355 3.3 35.2 1.0
O A:HOH382 3.3 32.5 1.0
CB B:SER167 3.5 29.0 1.0
CB A:SER167 3.6 32.5 1.0
O B:LEU171 3.6 31.0 1.0
O A:LEU171 3.6 33.1 1.0
CA B:SER167 3.7 30.0 1.0
CA A:SER167 3.8 31.7 1.0
NH2 B:ARG212 4.0 45.8 1.0
NH1 A:ARG212 4.1 48.5 1.0
O B:HOH310 4.5 30.3 1.0
O A:HOH324 4.6 39.3 1.0
N B:SER167 4.6 30.0 1.0
O B:SER167 4.7 32.3 1.0
C B:SER167 4.7 29.9 1.0
N A:SER167 4.7 31.0 1.0
O A:SER167 4.7 32.0 1.0
C A:SER167 4.8 32.3 1.0
C B:LEU171 4.8 31.0 1.0
C A:LEU171 4.8 32.3 1.0

Potassium binding site 3 out of 3 in 2fca

Go back to Potassium Binding Sites List in 2fca
Potassium binding site 3 out of 3 in the The Structure of Bstrmb


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of The Structure of Bstrmb within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K251

b:33.6
occ:1.00
O B:ASN115 2.5 30.9 1.0
O B:GLY46 2.5 34.1 1.0
O B:HOH423 2.6 46.7 1.0
O B:HOH261 2.9 26.5 1.0
O B:HOH469 2.9 45.5 1.0
O B:HOH315 3.0 31.6 1.0
O B:HOH408 3.2 48.3 1.0
C B:GLY46 3.6 33.4 1.0
C B:ASN115 3.7 30.8 1.0
CA B:GLY46 4.0 33.0 1.0
O B:VAL45 4.1 31.1 1.0
O B:HOH401 4.2 34.7 1.0
O B:PHE116 4.4 34.4 1.0
N B:ASN115 4.4 29.8 1.0
C B:PHE116 4.4 33.0 1.0
O B:HOH281 4.4 27.6 1.0
CA B:ASN115 4.4 31.1 1.0
CB B:ASN115 4.5 31.6 1.0
N B:SER117 4.5 32.0 1.0
CA B:SER117 4.6 31.4 1.0
OE1 B:GLU44 4.7 32.0 1.0
N B:PHE116 4.7 31.3 1.0
O B:HOH393 4.8 38.8 1.0
N B:THR47 4.8 34.2 1.0
N B:GLY46 4.9 33.1 1.0
OG B:SER117 5.0 29.5 1.0
C B:VAL45 5.0 31.3 1.0
CA B:PHE116 5.0 32.5 1.0

Reference:

I.Zegers, D.Gigot, F.Van Vliet, C.Tricot, S.Aymerich, J.M.Bujnicki, J.Kosinski, L.Droogmans. Crystal Structure of Bacillus Subtilis Trmb, the Trna (M7G46) Methyltransferase. Nucleic Acids Res. V. 34 1925 2006.
ISSN: ISSN 0305-1048
PubMed: 16600901
DOI: 10.1093/NAR/GKL116
Page generated: Sun Dec 13 23:09:33 2020

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