Sodium in PDB 2e7z: Acetylene Hydratase From Pelobacter Acetylenicus

All present enzymatic activity of Acetylene Hydratase From Pelobacter Acetylenicus:
4.2.1.71;

The structure of Acetylene Hydratase From Pelobacter Acetylenicus, PDB code: 2e7z was solved by O.Einsle, P.M.H.Kroneck, G.B.Seiffert, A.Messerschmidt, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.63 / 1.26
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	120.776, 71.971, 106.760, 90.00, 124.26, 90.00
R / Rfree (%)	16 / 19.5

The structure of Acetylene Hydratase From Pelobacter Acetylenicus also contains other interesting chemical elements:

Tungsten	(W)	1 atom
Iron	(Fe)	4 atoms

The binding sites of Sodium atom in the Acetylene Hydratase From Pelobacter Acetylenicus (pdb code 2e7z). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Acetylene Hydratase From Pelobacter Acetylenicus, PDB code: 2e7z:

Sodium binding site 1 out of 1 in the Acetylene Hydratase From Pelobacter Acetylenicus


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Acetylene Hydratase From Pelobacter Acetylenicus within 5.0Å range: probe atom residue distance (Å) B Occ A:Na1001 b:8.2 occ:1.00 OE2 A:GLU404 2.1 9.6 1.0 O A:HOH1144 2.1 11.7 1.0 O A:HOH1551 2.1 9.6 1.0 O A:ACT1003 2.1 9.8 1.0 O A:HOH1550 2.2 10.8 1.0 CD A:GLU404 3.1 10.1 1.0 C A:ACT1003 3.2 10.3 1.0 OXT A:ACT1003 3.4 10.2 1.0 OE1 A:GLU404 3.8 12.9 1.0 O A:HOH1492 4.0 12.9 1.0 NZ A:LYS410 4.0 14.0 1.0 CG A:GLU404 4.1 9.5 1.0 O A:HOH1748 4.1 19.0 1.0 O A:HOH1273 4.2 21.9 1.0 ND2 A:ASN435 4.3 8.2 1.0 OD1 A:ASN435 4.5 12.2 1.0 CH3 A:ACT1003 4.5 10.7 1.0 O A:HOH1193 4.7 19.0 1.0 CG A:ASN435 4.8 8.7 1.0 CE A:LYS410 5.0 11.7 1.0

G.B.Seiffert, G.M.Ullmann, A.Messerschmidt, B.Schink, P.M.H.Kroneck, O.Einsle. Structure of the Non-Redox-Active Tungsten/[4FE:4S] Enzyme Acetylene Hydratase Proc.Natl.Acad.Sci.Usa V. 104 3073 2007.
ISSN: ISSN 0027-8424
PubMed: 17360611
DOI: 10.1073/PNAS.0610407104