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Magnesium in PDB 2b3q: Crystal Structure of A Well-Folded Variant of Green Fluorescent Protein

Protein crystallography data

The structure of Crystal Structure of A Well-Folded Variant of Green Fluorescent Protein, PDB code: 2b3q was solved by J.D.Pedelacq, S.Cabantous, T.H.Tran, T.C.Terwilliger, G.S.Waldo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 85.407, 87.160, 145.647, 90.00, 90.00, 90.00
R / Rfree (%) 20.6 / 25.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of A Well-Folded Variant of Green Fluorescent Protein (pdb code 2b3q). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of A Well-Folded Variant of Green Fluorescent Protein, PDB code: 2b3q:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 2b3q

Go back to Magnesium Binding Sites List in 2b3q
Magnesium binding site 1 out of 3 in the Crystal Structure of A Well-Folded Variant of Green Fluorescent Protein


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of A Well-Folded Variant of Green Fluorescent Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg701

b:50.0
occ:1.00
ND2 A:ASN135 3.6 23.6 1.0
OD1 A:ASN135 3.8 26.5 1.0
CG A:ASN135 4.1 25.9 1.0
O A:HOH766 4.2 30.2 1.0
OG A:SER175 4.7 24.1 1.0
OD2 A:ASP173 4.8 35.0 1.0

Magnesium binding site 2 out of 3 in 2b3q

Go back to Magnesium Binding Sites List in 2b3q
Magnesium binding site 2 out of 3 in the Crystal Structure of A Well-Folded Variant of Green Fluorescent Protein


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of A Well-Folded Variant of Green Fluorescent Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg702

b:8.4
occ:1.00
O A:HOH724 3.1 26.8 1.0
NE A:ARG168 3.1 20.0 1.0
NH2 A:ARG168 3.1 19.4 1.0
NE D:ARG168 3.1 18.9 1.0
NH2 D:ARG168 3.2 16.0 1.0
O D:HOH252 3.2 15.6 1.0
CG A:ASN146 3.4 17.1 1.0
CZ A:ARG168 3.5 20.4 1.0
CG D:ASN146 3.5 14.0 1.0
OD1 A:ASN146 3.5 18.2 1.0
CZ D:ARG168 3.6 18.3 1.0
CB D:ASN146 3.7 13.9 1.0
CB A:ASN146 3.7 16.3 1.0
ND2 A:ASN146 3.8 13.4 1.0
ND2 D:ASN146 3.8 8.0 1.0
OD1 D:ASN146 3.8 13.0 1.0
CD A:ARG168 4.3 15.9 1.0
CD D:ARG168 4.3 17.4 1.0
O A:HOH794 4.5 34.6 1.0
NH1 A:ARG168 4.8 19.9 1.0
CB A:ARG168 4.8 15.2 1.0
CB D:ARG168 4.9 13.8 1.0
NH1 D:ARG168 4.9 13.9 1.0
OD1 A:ASN170 5.0 21.8 1.0
OD1 D:ASN170 5.0 25.6 1.0

Magnesium binding site 3 out of 3 in 2b3q

Go back to Magnesium Binding Sites List in 2b3q
Magnesium binding site 3 out of 3 in the Crystal Structure of A Well-Folded Variant of Green Fluorescent Protein


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of A Well-Folded Variant of Green Fluorescent Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg703

b:45.5
occ:1.00
OE1 C:GLU32 3.6 31.0 1.0
OD2 A:ASP19 4.0 30.2 1.0
O A:HOH752 4.1 39.1 1.0
OD1 A:ASP19 4.1 19.9 1.0
CG A:ASP19 4.5 23.4 1.0
O C:HOH274 4.7 24.3 1.0
CD C:GLU32 4.8 32.2 1.0

Reference:

J.D.Pedelacq, S.Cabantous, T.Tran, T.C.Terwilliger, G.S.Waldo. Engineering and Characterization of A Superfolder Green Fluorescent Protein. Nat.Biotechnol. V. 24 79 2006.
ISSN: ISSN 1087-0156
PubMed: 16369541
DOI: 10.1038/NBT1172
Page generated: Mon Dec 14 07:16:07 2020

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