Sodium in PDB 2jlm: Structure of A Putative Acetyltransferase (ACIAD1637) From Acinetobacter Baylyi ADP1

The structure of Structure of A Putative Acetyltransferase (ACIAD1637) From Acinetobacter Baylyi ADP1, PDB code: 2jlm was solved by A.M.Davies, R.Tata, A.Snape, B.J.Sutton, P.R.Brown, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	68.00 / 2.35
Space group	P 32
Cell size a, b, c (Å), α, β, γ (°)	78.410, 78.410, 197.760, 90.00, 90.00, 120.00
R / Rfree (%)	18.2 / 23.8

The binding sites of Sodium atom in the Structure of A Putative Acetyltransferase (ACIAD1637) From Acinetobacter Baylyi ADP1 (pdb code 2jlm). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Structure of A Putative Acetyltransferase (ACIAD1637) From Acinetobacter Baylyi ADP1, PDB code: 2jlm:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the Structure of A Putative Acetyltransferase (ACIAD1637) From Acinetobacter Baylyi ADP1


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structure of A Putative Acetyltransferase (ACIAD1637) From Acinetobacter Baylyi ADP1 within 5.0Å range: probe atom residue distance (Å) B Occ C:Na1191 b:38.3 occ:1.00 OH D:TYR88 3.0 30.3 1.0 O C:HOH2012 3.1 46.4 1.0 NH2 D:ARG83 3.2 21.3 1.0 O C:ACT1183 3.2 82.2 1.0 CE1 D:TYR88 3.6 22.9 1.0 CZ D:TYR88 3.7 21.3 1.0 SG C:CYS130 3.9 38.0 1.0 CD2 C:TYR39 3.9 19.7 1.0 CH3 C:ACT1183 4.0 51.5 1.0 C C:ACT1183 4.0 98.0 1.0 CG C:TYR39 4.0 23.2 1.0 O C:HOH2013 4.0 34.1 1.0 NE D:ARG83 4.0 21.5 1.0 CZ D:ARG83 4.1 19.4 1.0 CE2 C:TYR39 4.2 23.3 1.0 CD1 C:TYR39 4.4 30.9 1.0 CB C:TYR39 4.5 25.5 1.0 CZ C:TYR39 4.6 32.0 1.0 CB C:CYS130 4.6 26.5 1.0 O C:HOH2010 4.6 33.9 1.0 CE1 C:TYR39 4.7 17.9 1.0 CD1 D:PHE85 4.7 42.6 1.0 CD1 D:TYR88 4.8 15.3 1.0 CE1 D:PHE85 4.9 49.4 1.0 CG D:PHE85 5.0 39.6 1.0 OE2 C:GLU93 5.0 33.6 1.0

Sodium binding site 2 out of 2 in the Structure of A Putative Acetyltransferase (ACIAD1637) From Acinetobacter Baylyi ADP1


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Structure of A Putative Acetyltransferase (ACIAD1637) From Acinetobacter Baylyi ADP1 within 5.0Å range: probe atom residue distance (Å) B Occ E:Na1190 b:54.6 occ:1.00 OH F:TYR88 3.3 37.0 1.0 O E:HOH2020 3.3 35.5 1.0 O E:HOH2021 3.5 38.9 1.0 NH2 F:ARG83 3.5 23.2 1.0 SG E:CYS130 3.8 20.1 0.7 CD2 E:TYR39 3.8 31.5 1.0 CG E:TYR39 3.9 21.9 1.0 O E:HOH2018 3.9 38.0 1.0 CE2 E:TYR39 4.0 35.1 1.0 CE1 F:TYR88 4.1 23.0 1.0 CZ F:TYR88 4.1 21.8 1.0 O E:CYS130 4.2 20.6 0.3 CH3 E:ACT1183 4.2 55.6 1.0 O E:CYS130 4.2 20.6 0.7 CB E:CYS130 4.2 23.1 0.3 CD1 E:TYR39 4.3 28.7 1.0 CB E:CYS130 4.3 23.3 0.7 CZ E:TYR39 4.4 53.4 1.0 CZ F:ARG83 4.5 34.7 1.0 CE1 E:TYR39 4.5 22.0 1.0 NE F:ARG83 4.5 24.2 1.0 CB E:TYR39 4.5 22.6 1.0 C E:ACT1183 4.7 91.8 1.0 C E:CYS130 4.8 19.1 0.3 C E:CYS130 4.8 19.0 0.7 O E:ALA37 5.0 35.0 1.0

A.M.Davies, R.Tata, A.Snape, B.J.Sutton, P.R.Brown. Structure and Substrate Specificity of Acetyltransferase ACIAD1637 From Acinetobacter Baylyi ADP1. Biochimie V. 91 484 2009.
ISSN: ISSN 0300-9084
PubMed: 19135125
DOI: 10.1016/J.BIOCHI.2008.12.003