Aluminium in PDB 3puw: Crystal Structure of An Outward-Facing Mbp-Maltose Transporter Complex Bound to Adp-ALF4

All present enzymatic activity of Crystal Structure of An Outward-Facing Mbp-Maltose Transporter Complex Bound to Adp-ALF4:
3.6.3.19;

The structure of Crystal Structure of An Outward-Facing Mbp-Maltose Transporter Complex Bound to Adp-ALF4, PDB code: 3puw was solved by M.L.Oldham, J.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.99 / 2.30
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	81.881, 97.344, 112.336, 85.76, 79.42, 72.45
R / Rfree (%)	22 / 25.5

The structure of Crystal Structure of An Outward-Facing Mbp-Maltose Transporter Complex Bound to Adp-ALF4 also contains other interesting chemical elements:

Fluorine	(F)	8 atoms
Magnesium	(Mg)	2 atoms

The binding sites of Aluminium atom in the Crystal Structure of An Outward-Facing Mbp-Maltose Transporter Complex Bound to Adp-ALF4 (pdb code 3puw). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total 2 binding sites of Aluminium where determined in the Crystal Structure of An Outward-Facing Mbp-Maltose Transporter Complex Bound to Adp-ALF4, PDB code: 3puw:
Jump to Aluminium binding site number: 1; 2;

Aluminium binding site 1 out of 2 in the Crystal Structure of An Outward-Facing Mbp-Maltose Transporter Complex Bound to Adp-ALF4


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Crystal Structure of An Outward-Facing Mbp-Maltose Transporter Complex Bound to Adp-ALF4 within 5.0Å range: probe atom residue distance (Å) B Occ A:Al3001 b:20.8 occ:1.00 AL A:ALF3001 0.0 20.8 1.0 F2 A:ALF3001 1.8 19.9 1.0 F4 A:ALF3001 1.8 21.9 1.0 F3 A:ALF3001 1.8 21.2 1.0 F1 A:ALF3001 1.8 21.9 1.0 O3B A:ADP2501 2.0 25.0 1.0 O A:HOH384 2.3 13.4 1.0 PB A:ADP2501 3.2 27.1 1.0 MG A:MG1501 3.2 26.1 1.0 O2B A:ADP2501 3.5 26.4 1.0 N B:GLY137 3.7 21.9 1.0 OG B:SER135 3.8 24.6 1.0 OE2 A:GLU159 3.9 25.5 1.0 N A:GLY39 3.9 26.9 1.0 NE2 A:GLN82 4.0 24.7 1.0 O A:HOH382 4.0 20.0 1.0 NE2 A:HIS192 4.1 24.4 1.0 O A:HOH383 4.1 23.8 1.0 O1B A:ADP2501 4.1 27.7 1.0 CA B:GLY137 4.1 22.1 1.0 CB B:SER135 4.1 25.1 1.0 NZ A:LYS42 4.2 23.4 1.0 CA A:SER38 4.3 26.1 1.0 OG A:SER38 4.3 26.3 1.0 O B:ASN163 4.3 26.9 1.0 OE1 A:GLN82 4.4 26.4 1.0 O3A A:ADP2501 4.4 27.7 1.0 N B:GLY136 4.6 22.6 1.0 CD A:GLN82 4.6 24.9 1.0 CB A:SER38 4.6 26.2 1.0 C A:SER38 4.6 27.1 1.0 C B:GLY136 4.8 21.3 1.0 CE A:LYS42 4.8 23.7 1.0 CA A:GLY39 4.8 28.4 1.0 CE1 A:HIS192 4.8 24.8 1.0 CD A:GLU159 4.9 24.3 1.0 CA B:GLY136 4.9 21.4 1.0

Aluminium binding site 2 out of 2 in the Crystal Structure of An Outward-Facing Mbp-Maltose Transporter Complex Bound to Adp-ALF4


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 2 of Crystal Structure of An Outward-Facing Mbp-Maltose Transporter Complex Bound to Adp-ALF4 within 5.0Å range: probe atom residue distance (Å) B Occ B:Al3002 b:27.9 occ:1.00 AL B:ALF3002 0.0 27.9 1.0 F4 B:ALF3002 1.8 29.0 1.0 F1 B:ALF3002 1.8 28.8 1.0 F2 B:ALF3002 1.8 28.9 1.0 F3 B:ALF3002 1.8 29.9 1.0 O3B B:ADP2502 2.1 32.0 1.0 O B:HOH384 2.3 31.1 1.0 MG B:MG1502 3.2 22.9 1.0 PB B:ADP2502 3.4 34.1 1.0 N A:GLY137 3.6 30.4 1.0 OG A:SER135 3.7 34.3 1.0 OE2 B:GLU159 3.7 28.6 1.0 N B:GLY39 3.8 37.6 1.0 O2B B:ADP2502 3.8 32.1 1.0 NE2 B:GLN82 3.9 27.7 1.0 CA A:GLY137 4.0 30.4 1.0 NE2 B:HIS192 4.0 34.5 1.0 OG B:SER38 4.1 36.3 1.0 O B:HOH382 4.1 29.8 1.0 CB A:SER135 4.1 34.9 1.0 CA B:SER38 4.2 37.1 1.0 NZ B:LYS42 4.2 36.0 1.0 O A:ASN163 4.2 31.1 1.0 O B:HOH383 4.3 36.3 1.0 O1B B:ADP2502 4.3 34.8 1.0 O3A B:ADP2502 4.4 35.3 1.0 C B:SER38 4.5 38.4 1.0 N A:GLY136 4.6 31.2 1.0 CB B:SER38 4.6 36.9 1.0 OE1 B:GLN82 4.6 28.2 1.0 CA B:GLY39 4.7 39.0 1.0 CE B:LYS42 4.7 34.9 1.0 CD B:GLN82 4.7 27.5 1.0 C A:GLY136 4.8 29.6 1.0 CD B:GLU159 4.9 28.6 1.0 CE1 B:HIS192 4.9 35.0 1.0 CD2 B:HIS192 4.9 32.9 1.0 CA A:GLY136 5.0 29.6 1.0

M.L.Oldham, J.Chen. Snapshots of the Maltose Transporter During Atp Hydrolysis. Proc.Natl.Acad.Sci.Usa V. 108 15152 2011.
ISSN: ISSN 0027-8424
PubMed: 21825153
DOI: 10.1073/PNAS.1108858108