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Vanadium in PDB 6mhz: Vanadate Trapped Cryo-Em Structure of E.Coli LPTB2FG Transporter

Vanadium Binding Sites:

The binding sites of Vanadium atom in the Vanadate Trapped Cryo-Em Structure of E.Coli LPTB2FG Transporter (pdb code 6mhz). This binding sites where shown within 5.0 Angstroms radius around Vanadium atom.
In total 2 binding sites of Vanadium where determined in the Vanadate Trapped Cryo-Em Structure of E.Coli LPTB2FG Transporter, PDB code: 6mhz:
Jump to Vanadium binding site number: 1; 2;

Vanadium binding site 1 out of 2 in 6mhz

Go back to Vanadium Binding Sites List in 6mhz
Vanadium binding site 1 out of 2 in the Vanadate Trapped Cryo-Em Structure of E.Coli LPTB2FG Transporter


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 1 of Vanadate Trapped Cryo-Em Structure of E.Coli LPTB2FG Transporter within 5.0Å range:
probe atom residue distance (Å) B Occ
A:V301

b:19.7
occ:1.00
VG A:AOV301 0.0 19.7 1.0
O3G A:AOV301 2.1 19.7 1.0
O2G A:AOV301 2.1 19.7 1.0
O4G A:AOV301 2.1 19.7 1.0
O1G A:AOV301 2.1 19.7 1.0
O3B A:AOV301 2.1 19.7 1.0
O2B A:AOV301 2.9 19.7 1.0
PB A:AOV301 3.1 19.7 1.0
O1B A:AOV301 3.7 19.7 1.0
NE2 A:HIS195 3.9 19.8 1.0
O B:GLY167 3.9 19.0 1.0
CA A:ASN38 4.0 23.3 1.0
NE2 A:GLN85 4.0 15.8 1.0
N B:GLY141 4.0 20.0 1.0
CB A:ASN38 4.2 23.3 1.0
OE2 A:GLU163 4.2 16.6 1.0
OG B:SER139 4.2 19.6 1.0
CA B:GLY141 4.4 20.0 1.0
O3A A:AOV301 4.5 19.7 1.0
CE1 A:HIS195 4.7 19.8 1.0
N A:GLY39 4.7 21.5 1.0
O A:PRO37 4.8 20.3 1.0
N A:ASN38 4.8 23.3 1.0
CD2 A:HIS195 4.8 19.8 1.0
CD A:LYS42 4.9 16.9 1.0
C A:ASN38 4.9 23.3 1.0
N B:GLY140 5.0 18.9 1.0

Vanadium binding site 2 out of 2 in 6mhz

Go back to Vanadium Binding Sites List in 6mhz
Vanadium binding site 2 out of 2 in the Vanadate Trapped Cryo-Em Structure of E.Coli LPTB2FG Transporter


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 2 of Vanadate Trapped Cryo-Em Structure of E.Coli LPTB2FG Transporter within 5.0Å range:
probe atom residue distance (Å) B Occ
B:V301

b:19.1
occ:1.00
VG B:AOV301 0.0 19.1 1.0
O2G B:AOV301 2.1 19.1 1.0
O1G B:AOV301 2.1 19.1 1.0
O4G B:AOV301 2.1 19.1 1.0
O3B B:AOV301 2.1 19.1 1.0
O3G B:AOV301 2.1 19.1 1.0
NZ B:LYS42 2.9 19.1 1.0
O2B B:AOV301 3.0 19.1 1.0
PB B:AOV301 3.1 19.1 1.0
ND2 B:ASN38 3.4 19.6 1.0
NE2 B:HIS195 3.7 21.5 1.0
O1B B:AOV301 3.9 19.1 1.0
O A:SER139 4.0 18.8 1.0
OE2 B:GLU163 4.0 21.5 1.0
CE B:LYS42 4.2 19.1 1.0
N B:GLY39 4.3 17.3 1.0
NE2 B:GLN85 4.4 18.5 1.0
CD2 B:HIS195 4.4 21.5 1.0
O3A B:AOV301 4.4 19.1 1.0
O A:GLY167 4.5 18.8 1.0
N A:GLY141 4.5 20.1 1.0
CA B:ASN38 4.6 19.6 1.0
CG B:ASN38 4.6 19.6 1.0
OG A:SER139 4.7 18.8 1.0
CE1 B:HIS195 4.7 21.5 1.0
O B:PRO37 4.8 19.2 1.0
C A:SER139 4.8 18.8 1.0
OE1 B:GLN85 4.9 18.5 1.0
C B:ASN38 5.0 19.6 1.0

Reference:

Y.Li, B.J.Orlando, M.Liao. Structural Basis of Lipopolysaccharide Extraction By the LPTB2FGC Complex. Nature V. 567 486 2019.
ISSN: ESSN 1476-4687
PubMed: 30894744
DOI: 10.1038/S41586-019-1025-6
Page generated: Fri Oct 11 20:06:41 2024

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