Vanadium in PDB 3p20: Crystal Structure of Vanadate Bound Subunit A of the A1AO Atp Synthase

All present enzymatic activity of Crystal Structure of Vanadate Bound Subunit A of the A1AO Atp Synthase:
3.6.3.14;

The structure of Crystal Structure of Vanadate Bound Subunit A of the A1AO Atp Synthase, PDB code: 3p20 was solved by M.S.S.Manimekalai, A.Kumar, J.Jeyakanthan, G.Gruber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.25 / 2.85
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	127.550, 127.550, 104.064, 90.00, 90.00, 90.00
R / Rfree (%)	21 / 24.6

The binding sites of Vanadium atom in the Crystal Structure of Vanadate Bound Subunit A of the A1AO Atp Synthase (pdb code 3p20). This binding sites where shown within 5.0 Angstroms radius around Vanadium atom.
In total 2 binding sites of Vanadium where determined in the Crystal Structure of Vanadate Bound Subunit A of the A1AO Atp Synthase, PDB code: 3p20:
Jump to Vanadium binding site number: 1; 2;

Vanadium binding site 1 out of 2 in the Crystal Structure of Vanadate Bound Subunit A of the A1AO Atp Synthase


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 1 of Crystal Structure of Vanadate Bound Subunit A of the A1AO Atp Synthase within 5.0Å range: probe atom residue distance (Å) B Occ A:V589 b:81.8 occ:1.00 V A:VO4589 0.0 81.8 1.0 O2 A:VO4589 1.9 81.2 1.0 O1 A:VO4589 1.9 80.1 1.0 O3 A:VO4589 1.9 82.0 1.0 O4 A:VO4589 1.9 81.0 1.0 OG A:SER238 4.2 39.2 1.0 CG2 A:THR241 4.3 36.6 1.0 CB A:LYS240 4.3 38.5 1.0 CB A:LEU417 4.8 28.8 1.0 CD2 A:LEU417 4.8 26.9 1.0 CB A:SER238 4.9 38.1 1.0 CG A:LEU417 4.9 29.4 1.0 OG1 A:THR241 5.0 36.1 1.0

Vanadium binding site 2 out of 2 in the Crystal Structure of Vanadate Bound Subunit A of the A1AO Atp Synthase


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 2 of Crystal Structure of Vanadate Bound Subunit A of the A1AO Atp Synthase within 5.0Å range: probe atom residue distance (Å) B Occ A:V590 b:86.0 occ:1.00 V A:VO4590 0.0 86.0 1.0 O2 A:VO4590 1.9 84.0 1.0 O1 A:VO4590 1.9 83.9 1.0 O4 A:VO4590 1.9 85.2 1.0 O3 A:VO4590 1.9 85.8 1.0 O A:LEU417 3.3 28.2 1.0 C A:LEU417 4.4 28.1 1.0 O A:HOH623 4.6 42.1 1.0 CA A:ASP418 4.6 30.8 1.0 CE1 A:PHE399 4.8 65.2 1.0 CG A:PRO233 4.9 33.8 1.0 CZ A:PHE399 4.9 64.4 1.0 O A:HOH624 5.0 37.5 1.0 CB A:ASP418 5.0 30.6 1.0

M.S.Manimekalai, A.Kumar, J.Jeyakanthan, G.Gruber. The Transition-Like State and Pi Entrance Into the Catalytic A Subunit of the Biological Engine A-Atp Synthase. J.Mol.Biol. V. 408 736 2011.
ISSN: ISSN 0022-2836
PubMed: 21396943
DOI: 10.1016/J.JMB.2011.03.010