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Vanadium in PDB 3puv: Crystal Structure of An Outward-Facing Mbp-Maltose Transporter Complex Bound to Adp-VO4

Enzymatic activity of Crystal Structure of An Outward-Facing Mbp-Maltose Transporter Complex Bound to Adp-VO4

All present enzymatic activity of Crystal Structure of An Outward-Facing Mbp-Maltose Transporter Complex Bound to Adp-VO4:
3.6.3.19;

Protein crystallography data

The structure of Crystal Structure of An Outward-Facing Mbp-Maltose Transporter Complex Bound to Adp-VO4, PDB code: 3puv 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) 20.00 / 2.40
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 81.786, 97.125, 112.791, 85.58, 78.71, 72.69
R / Rfree (%) 22.3 / 25.3

Other elements in 3puv:

The structure of Crystal Structure of An Outward-Facing Mbp-Maltose Transporter Complex Bound to Adp-VO4 also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Vanadium Binding Sites:

The binding sites of Vanadium atom in the Crystal Structure of An Outward-Facing Mbp-Maltose Transporter Complex Bound to Adp-VO4 (pdb code 3puv). 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 An Outward-Facing Mbp-Maltose Transporter Complex Bound to Adp-VO4, PDB code: 3puv:
Jump to Vanadium binding site number: 1; 2;

Vanadium binding site 1 out of 2 in 3puv

Go back to Vanadium Binding Sites List in 3puv
Vanadium binding site 1 out of 2 in the Crystal Structure of An Outward-Facing Mbp-Maltose Transporter Complex Bound to Adp-VO4


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 An Outward-Facing Mbp-Maltose Transporter Complex Bound to Adp-VO4 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:V3001

b:20.4
occ:1.00
V A:VO43001 0.0 20.4 1.0
O3 A:VO43001 1.7 19.2 1.0
O2 A:VO43001 1.7 21.8 1.0
O1 A:VO43001 1.7 20.7 1.0
O3B A:ADP2501 2.0 22.0 1.0
O4 A:VO43001 2.1 18.7 1.0
PB A:ADP2501 3.3 22.5 1.0
MG A:MG1501 3.4 17.8 1.0
OE2 A:GLU159 3.5 33.3 1.0
O A:HOH383 3.7 15.9 1.0
O2B A:ADP2501 3.7 21.3 1.0
N A:GLY39 3.9 25.5 1.0
N B:GLY137 3.9 23.2 1.0
NE2 A:HIS192 4.0 27.0 1.0
OG B:SER135 4.0 26.9 1.0
O A:HOH382 4.1 16.2 1.0
NE2 A:GLN82 4.2 24.3 1.0
OG A:SER38 4.2 25.5 1.0
CA A:SER38 4.2 25.5 1.0
O1B A:ADP2501 4.2 22.7 1.0
CB B:SER135 4.2 27.4 1.0
NZ A:LYS42 4.3 24.7 1.0
O3A A:ADP2501 4.3 24.0 1.0
N B:GLY136 4.4 24.2 1.0
CA B:GLY137 4.5 23.0 1.0
O B:ASN163 4.5 28.1 1.0
C A:SER38 4.6 26.3 1.0
OE1 A:GLN82 4.6 25.9 1.0
CB A:SER38 4.6 25.8 1.0
CE A:LYS42 4.6 24.1 1.0
CD A:GLU159 4.6 32.4 1.0
CE1 A:HIS192 4.6 27.6 1.0
CD A:GLN82 4.8 24.7 1.0
CA A:GLY39 4.8 26.7 1.0
CA B:GLY136 4.9 22.8 1.0
C B:GLY136 4.9 22.5 1.0

Vanadium binding site 2 out of 2 in 3puv

Go back to Vanadium Binding Sites List in 3puv
Vanadium binding site 2 out of 2 in the Crystal Structure of An Outward-Facing Mbp-Maltose Transporter Complex Bound to Adp-VO4


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 An Outward-Facing Mbp-Maltose Transporter Complex Bound to Adp-VO4 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:V3002

b:31.5
occ:1.00
V B:VO43002 0.0 31.5 1.0
O1 B:VO43002 1.7 31.9 1.0
O2 B:VO43002 1.7 31.5 1.0
O3 B:VO43002 1.7 29.8 1.0
O3B B:ADP2502 2.1 34.0 1.0
O4 B:VO43002 2.1 29.4 1.0
MG B:MG1502 3.3 28.6 1.0
PB B:ADP2502 3.4 34.9 1.0
OE2 B:GLU159 3.6 34.3 1.0
N B:GLY39 3.8 38.8 1.0
O2B B:ADP2502 3.8 33.4 1.0
O B:HOH382 3.8 35.6 1.0
N A:GLY137 3.8 32.1 1.0
OG B:SER38 3.9 36.4 1.0
OG A:SER135 4.0 36.3 1.0
NZ B:LYS42 4.1 35.3 1.0
NE2 B:GLN82 4.1 35.0 1.0
NE2 B:HIS192 4.1 36.7 1.0
CA B:SER38 4.1 37.9 1.0
CB A:SER135 4.1 35.6 1.0
O1B B:ADP2502 4.3 37.5 1.0
CA A:GLY137 4.4 32.6 1.0
O B:HOH383 4.4 28.1 1.0
O3A B:ADP2502 4.4 37.3 1.0
N A:GLY136 4.4 32.2 1.0
CB B:SER38 4.5 37.3 1.0
C B:SER38 4.5 39.7 1.0
O A:ASN163 4.5 33.6 1.0
CA B:GLY39 4.7 40.7 1.0
CE B:LYS42 4.8 34.3 1.0
CD B:GLU159 4.8 33.3 1.0
C A:GLY136 4.9 31.1 1.0
CE1 B:HIS192 4.9 38.1 1.0
OE1 B:GLN82 4.9 35.1 1.0
CD B:GLN82 4.9 34.4 1.0
CA A:GLY136 5.0 30.9 1.0

Reference:

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
Page generated: Thu Oct 29 07:05:13 2020

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