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Magnesium in PDB 2fna: Crystal Structure of An Archaeal Aaa+ Atpase (SSO1545) From Sulfolobus Solfataricus P2 at 2.00 A Resolution

Protein crystallography data

The structure of Crystal Structure of An Archaeal Aaa+ Atpase (SSO1545) From Sulfolobus Solfataricus P2 at 2.00 A Resolution, PDB code: 2fna was solved by Joint Center For Structural Genomics (Jcsg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 69.50 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 55.360, 108.350, 70.570, 90.00, 100.31, 90.00
R / Rfree (%) 17.4 / 22.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of An Archaeal Aaa+ Atpase (SSO1545) From Sulfolobus Solfataricus P2 at 2.00 A Resolution (pdb code 2fna). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of An Archaeal Aaa+ Atpase (SSO1545) From Sulfolobus Solfataricus P2 at 2.00 A Resolution, PDB code: 2fna:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 2fna

Go back to Magnesium Binding Sites List in 2fna
Magnesium binding site 1 out of 2 in the Crystal Structure of An Archaeal Aaa+ Atpase (SSO1545) From Sulfolobus Solfataricus P2 at 2.00 A Resolution


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 An Archaeal Aaa+ Atpase (SSO1545) From Sulfolobus Solfataricus P2 at 2.00 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg400

b:27.5
occ:1.00
O A:HOH637 2.0 28.4 1.0
O3B A:ADP500 2.0 18.4 1.0
O A:HOH670 2.1 24.5 1.0
O A:HOH668 2.1 27.6 1.0
O A:HOH669 2.1 29.3 1.0
OG A:SER43 2.2 35.0 1.0
CB A:SER43 3.2 33.8 1.0
PB A:ADP500 3.2 22.9 1.0
O2B A:ADP500 3.5 24.7 1.0
N A:SER43 3.9 32.7 1.0
O2A A:ADP500 4.0 26.6 1.0
OD1 A:ASP143 4.1 36.0 1.0
CA A:SER43 4.1 31.7 1.0
OE2 A:GLU144 4.1 39.8 1.0
OD2 A:ASP143 4.2 31.6 1.0
O1B A:ADP500 4.3 24.5 1.0
O3A A:ADP500 4.3 25.8 1.0
O A:HOH643 4.5 44.8 1.0
CG A:ASP143 4.5 36.2 1.0
PA A:ADP500 4.6 27.8 1.0
O A:HOH519 4.6 34.3 1.0
O A:HOH645 4.8 38.0 1.0
O1A A:ADP500 4.9 26.2 1.0
CG A:GLU144 4.9 33.9 1.0
C A:LYS42 5.0 29.7 1.0

Magnesium binding site 2 out of 2 in 2fna

Go back to Magnesium Binding Sites List in 2fna
Magnesium binding site 2 out of 2 in the Crystal Structure of An Archaeal Aaa+ Atpase (SSO1545) From Sulfolobus Solfataricus P2 at 2.00 A Resolution


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 An Archaeal Aaa+ Atpase (SSO1545) From Sulfolobus Solfataricus P2 at 2.00 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg400

b:24.5
occ:1.00
O B:HOH684 2.0 22.7 1.0
OG B:SER43 2.1 31.1 1.0
O3B B:ADP500 2.1 22.8 1.0
O B:HOH666 2.1 24.9 1.0
O B:HOH683 2.1 29.5 1.0
O B:HOH667 2.2 25.5 1.0
CB B:SER43 3.2 32.6 1.0
PB B:ADP500 3.3 24.2 1.0
O2B B:ADP500 3.6 24.8 1.0
OD1 B:ASP143 3.9 32.4 1.0
OE2 B:GLU144 3.9 40.1 1.0
N B:SER43 4.0 31.8 1.0
CA B:SER43 4.1 30.7 1.0
O2A B:ADP500 4.2 29.7 1.0
OD2 B:ASP143 4.3 34.6 1.0
O1B B:ADP500 4.4 22.9 1.0
O B:HOH611 4.4 46.4 1.0
O3A B:ADP500 4.4 21.7 1.0
CG B:ASP143 4.5 37.1 1.0
NH1 B:ARG63 4.5 64.3 1.0
PA B:ADP500 4.6 22.9 1.0
O B:HOH627 4.7 53.4 1.0
O B:HOH515 4.7 29.2 1.0
O B:HOH516 4.8 33.6 1.0
CD B:GLU144 4.8 33.3 1.0
CG B:GLU144 4.9 26.8 1.0
CD B:ARG63 4.9 65.0 1.0
CB B:LYS42 5.0 29.9 1.0

Reference:

Q.Xu, C.L.Rife, D.Carlton, M.D.Miller, S.S.Krishna, M.A.Elsliger, P.Abdubek, T.Astakhova, H.J.Chiu, T.Clayton, L.Duan, J.Feuerhelm, S.K.Grzechnik, J.Hale, G.W.Han, L.Jaroszewski, K.K.Jin, H.E.Klock, M.W.Knuth, A.Kumar, D.Mcmullan, A.T.Morse, E.Nigoghossian, L.Okach, S.Oommachen, J.Paulsen, R.Reyes, H.Van Den Bedem, K.O.Hodgson, J.Wooley, A.M.Deacon, A.Godzik, S.A.Lesley, I.A.Wilson. Crystal Structure of A Novel Archaeal Aaa+ Atpase SSO1545 From Sulfolobus Solfataricus. Proteins V. 74 1041 2009.
ISSN: ISSN 0887-3585
PubMed: 19089981
DOI: 10.1002/PROT.22325
Page generated: Mon Dec 14 07:23:22 2020

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