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Magnesium in PDB 5acp: W228R-Investigation of the Impact From Residues W228 and Y233 in the Metallo-Beta-Lactamase Gim-1

Protein crystallography data

The structure of W228R-Investigation of the Impact From Residues W228 and Y233 in the Metallo-Beta-Lactamase Gim-1, PDB code: 5acp was solved by S.Skagseth, T.J.Carlsen, G.E.K.Bjerga, J.Spencer, O.Samuelsen, H.-K.S.Leiros, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.83 / 1.98
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 38.757, 133.619, 40.702, 90.00, 95.26, 90.00
R / Rfree (%) 20.2 / 23.4

Other elements in 5acp:

The structure of W228R-Investigation of the Impact From Residues W228 and Y233 in the Metallo-Beta-Lactamase Gim-1 also contains other interesting chemical elements:

Zinc (Zn) 3 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the W228R-Investigation of the Impact From Residues W228 and Y233 in the Metallo-Beta-Lactamase Gim-1 (pdb code 5acp). 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 W228R-Investigation of the Impact From Residues W228 and Y233 in the Metallo-Beta-Lactamase Gim-1, PDB code: 5acp:

Magnesium binding site 1 out of 1 in 5acp

Go back to Magnesium Binding Sites List in 5acp
Magnesium binding site 1 out of 1 in the W228R-Investigation of the Impact From Residues W228 and Y233 in the Metallo-Beta-Lactamase Gim-1


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of W228R-Investigation of the Impact From Residues W228 and Y233 in the Metallo-Beta-Lactamase Gim-1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1298

b:42.0
occ:1.00
OG A:SER139 2.5 30.5 1.0
O A:ASP199 2.7 35.9 1.0
HB2 A:ASP199 2.8 42.7 1.0
O A:HOH2099 2.8 34.5 1.0
HG A:SER139 2.9 36.6 1.0
HB3 A:LEU141 2.9 46.0 1.0
HA A:ASP199 2.9 42.0 1.0
HD21 A:LEU141 3.3 50.3 1.0
CB A:SER139 3.3 32.4 1.0
HG21 A:ILE201 3.3 39.1 1.0
HB2 A:SER139 3.3 38.9 1.0
HB3 A:SER139 3.3 38.9 1.0
C A:ASP199 3.4 33.4 1.0
CA A:ASP199 3.4 35.0 1.0
HD1 A:TYR191 3.5 47.2 1.0
CB A:ASP199 3.5 35.6 1.0
H A:THR142 3.7 40.9 1.0
CD1 A:TYR191 3.8 39.3 1.0
OG1 A:THR142 3.9 31.5 1.0
CG2 A:ILE201 3.9 32.6 1.0
HG22 A:ILE201 3.9 39.1 1.0
CB A:LEU141 3.9 38.4 1.0
HB3 A:ASP199 3.9 42.7 1.0
HG23 A:ILE201 3.9 39.1 1.0
HE1 A:TYR191 4.0 48.3 1.0
HG1 A:THR142 4.0 37.8 1.0
O A:HOH2053 4.1 38.7 1.0
CE1 A:TYR191 4.1 40.2 1.0
CD2 A:LEU141 4.1 41.9 1.0
HB2 A:LEU141 4.3 46.0 1.0
HG A:LEU141 4.3 47.8 1.0
HB2 A:TYR191 4.3 48.4 1.0
N A:THR142 4.3 34.1 1.0
H A:LEU141 4.3 42.6 1.0
CG A:LEU141 4.4 39.8 1.0
HD23 A:LEU141 4.5 50.3 1.0
CG A:TYR191 4.6 40.2 1.0
N A:ASN200 4.7 32.8 1.0
CA A:SER139 4.7 33.5 1.0
O A:HOH2037 4.7 29.9 1.0
CG A:ASP199 4.7 38.2 1.0
CA A:LEU141 4.8 36.3 1.0
HD22 A:LEU141 4.8 50.3 1.0
N A:ASP199 4.8 33.5 1.0
N A:LEU141 4.9 35.5 1.0
H A:SER139 4.9 41.4 1.0
CB A:THR142 4.9 32.4 1.0
CB A:TYR191 5.0 40.3 1.0
C A:LEU141 5.0 35.2 1.0

Reference:

S.Skagseth, T.J.Carlsen, G.E.K.Bjerga, J.Spencer, O.Samuelsen, H.S.Leiros. Role of Residues W228 and Y233 in the Structure and Activity of Metallo-Beta-Lactamase Gim-1. Antimicrob.Agents Chemother. V. 60 990 2015.
ISSN: ISSN 0066-4804
PubMed: 26643332
DOI: 10.1128/AAC.02017-15
Page generated: Sun Sep 29 00:30:49 2024

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