Mercury in PDB 6cvl: Crystal Structure of the Escherichia Coli Atpgs-Bound Metni Methionine Abc Transporter in Complex with Its Metq Binding Protein
Protein crystallography data
The structure of Crystal Structure of the Escherichia Coli Atpgs-Bound Metni Methionine Abc Transporter in Complex with Its Metq Binding Protein, PDB code: 6cvl
was solved by
P.T.Nguyen,
J.T.Kaiser,
D.C.Rees,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
39.85 /
2.95
|
Space group
|
P 32 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
107.960,
107.960,
354.520,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
20.8 /
22.6
|
Other elements in 6cvl:
The structure of Crystal Structure of the Escherichia Coli Atpgs-Bound Metni Methionine Abc Transporter in Complex with Its Metq Binding Protein also contains other interesting chemical elements:
Mercury Binding Sites:
The binding sites of Mercury atom in the Crystal Structure of the Escherichia Coli Atpgs-Bound Metni Methionine Abc Transporter in Complex with Its Metq Binding Protein
(pdb code 6cvl). This binding sites where shown within
5.0 Angstroms radius around Mercury atom.
In total 3 binding sites of Mercury where determined in the
Crystal Structure of the Escherichia Coli Atpgs-Bound Metni Methionine Abc Transporter in Complex with Its Metq Binding Protein, PDB code: 6cvl:
Jump to Mercury binding site number:
1;
2;
3;
Mercury binding site 1 out
of 3 in 6cvl
Go back to
Mercury Binding Sites List in 6cvl
Mercury binding site 1 out
of 3 in the Crystal Structure of the Escherichia Coli Atpgs-Bound Metni Methionine Abc Transporter in Complex with Its Metq Binding Protein
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 1 of Crystal Structure of the Escherichia Coli Atpgs-Bound Metni Methionine Abc Transporter in Complex with Its Metq Binding Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Hg401
b:0.3
occ:1.00
|
HE1
|
C:HIS0
|
2.7
|
0.6
|
1.0
|
CE1
|
C:HIS0
|
3.2
|
0.2
|
1.0
|
ND1
|
C:HIS0
|
3.3
|
0.5
|
1.0
|
H1
|
C:HIS0
|
3.5
|
0.2
|
1.0
|
N
|
C:HIS0
|
4.4
|
0.1
|
1.0
|
NE2
|
C:HIS0
|
4.4
|
0.9
|
1.0
|
H3
|
C:HIS0
|
4.6
|
0.2
|
1.0
|
CG
|
C:HIS0
|
4.6
|
0.1
|
1.0
|
HB3
|
C:PRO29
|
4.7
|
97.5
|
1.0
|
H2
|
C:HIS0
|
4.8
|
0.2
|
1.0
|
HE2
|
C:HIS0
|
4.9
|
0.3
|
1.0
|
|
Mercury binding site 2 out
of 3 in 6cvl
Go back to
Mercury Binding Sites List in 6cvl
Mercury binding site 2 out
of 3 in the Crystal Structure of the Escherichia Coli Atpgs-Bound Metni Methionine Abc Transporter in Complex with Its Metq Binding Protein
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 2 of Crystal Structure of the Escherichia Coli Atpgs-Bound Metni Methionine Abc Transporter in Complex with Its Metq Binding Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Hg402
b:0.8
occ:1.00
|
HG
|
C:CYS164
|
2.0
|
81.3
|
1.0
|
HB3
|
C:ALA167
|
2.8
|
75.0
|
1.0
|
SG
|
C:CYS164
|
3.0
|
70.1
|
1.0
|
HD11
|
C:LEU183
|
3.1
|
0.0
|
1.0
|
HB3
|
C:CYS164
|
3.1
|
85.9
|
1.0
|
CB
|
C:CYS164
|
3.5
|
73.0
|
1.0
|
HD13
|
C:LEU183
|
3.5
|
0.0
|
1.0
|
HB2
|
C:CYS164
|
3.5
|
85.9
|
1.0
|
CD1
|
C:LEU183
|
3.7
|
98.1
|
1.0
|
CB
|
C:ALA167
|
3.8
|
60.1
|
1.0
|
HB2
|
C:LEU196
|
3.8
|
83.1
|
1.0
|
HD22
|
C:LEU196
|
3.8
|
86.7
|
1.0
|
HG23
|
C:THR168
|
3.8
|
78.9
|
1.0
|
HB2
|
C:ALA167
|
4.0
|
75.0
|
1.0
|
HD12
|
C:LEU183
|
4.0
|
0.0
|
1.0
|
HB3
|
C:LEU196
|
4.0
|
83.1
|
1.0
|
H
|
C:ALA167
|
4.1
|
76.5
|
1.0
|
HB1
|
C:ALA167
|
4.1
|
75.0
|
1.0
|
HD21
|
C:LEU180
|
4.2
|
0.0
|
1.0
|
HD23
|
C:LEU180
|
4.3
|
0.0
|
1.0
|
CB
|
C:LEU196
|
4.3
|
69.5
|
1.0
|
HD11
|
C:ILE207
|
4.6
|
0.8
|
1.0
|
CD2
|
C:LEU180
|
4.6
|
95.6
|
1.0
|
HG21
|
C:ILE194
|
4.6
|
84.4
|
1.0
|
CD2
|
C:LEU196
|
4.7
|
74.9
|
1.0
|
HD22
|
C:LEU180
|
4.7
|
0.0
|
1.0
|
CG2
|
C:THR168
|
4.7
|
67.8
|
1.0
|
HG21
|
C:THR168
|
4.7
|
78.9
|
1.0
|
HD21
|
C:LEU183
|
4.7
|
0.2
|
1.0
|
HD12
|
C:ILE87
|
4.7
|
70.4
|
1.0
|
CA
|
C:ALA167
|
4.8
|
59.7
|
1.0
|
N
|
C:ALA167
|
4.8
|
60.2
|
1.0
|
HD13
|
C:LEU196
|
4.9
|
85.4
|
1.0
|
HD23
|
C:LEU196
|
4.9
|
86.7
|
1.0
|
CA
|
C:CYS164
|
5.0
|
73.8
|
1.0
|
HD22
|
C:LEU183
|
5.0
|
0.2
|
1.0
|
HG11
|
C:VAL203
|
5.0
|
88.0
|
1.0
|
HD21
|
C:LEU162
|
5.0
|
0.9
|
1.0
|
CG
|
C:LEU183
|
5.0
|
95.4
|
1.0
|
|
Mercury binding site 3 out
of 3 in 6cvl
Go back to
Mercury Binding Sites List in 6cvl
Mercury binding site 3 out
of 3 in the Crystal Structure of the Escherichia Coli Atpgs-Bound Metni Methionine Abc Transporter in Complex with Its Metq Binding Protein
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 3 of Crystal Structure of the Escherichia Coli Atpgs-Bound Metni Methionine Abc Transporter in Complex with Its Metq Binding Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Hg401
b:0.9
occ:1.00
|
I
|
D:IOD403
|
2.5
|
0.6
|
1.0
|
HB3
|
D:ALA167
|
3.1
|
79.8
|
1.0
|
H
|
D:ALA167
|
3.3
|
77.6
|
1.0
|
HD22
|
D:LEU196
|
3.4
|
80.0
|
1.0
|
HG1
|
D:THR168
|
3.4
|
78.5
|
1.0
|
HB2
|
D:LEU196
|
3.4
|
78.3
|
1.0
|
HB3
|
D:CYS164
|
3.4
|
75.2
|
1.0
|
HD13
|
D:LEU196
|
3.6
|
79.7
|
1.0
|
HG11
|
D:VAL203
|
3.6
|
86.8
|
1.0
|
HG
|
D:CYS164
|
3.7
|
80.8
|
1.0
|
HB2
|
D:CYS164
|
3.7
|
75.2
|
1.0
|
CB
|
D:CYS164
|
3.9
|
58.3
|
1.0
|
HD21
|
D:LEU180
|
3.9
|
93.0
|
1.0
|
N
|
D:ALA167
|
4.0
|
66.1
|
1.0
|
CB
|
D:ALA167
|
4.0
|
68.9
|
1.0
|
H
|
D:THR168
|
4.1
|
77.2
|
1.0
|
I
|
D:IOD402
|
4.2
|
0.8
|
1.0
|
CB
|
D:LEU196
|
4.2
|
59.2
|
1.0
|
OG1
|
D:THR168
|
4.2
|
73.8
|
1.0
|
SG
|
D:CYS164
|
4.2
|
65.1
|
1.0
|
CD2
|
D:LEU196
|
4.3
|
62.7
|
1.0
|
HB3
|
D:LEU196
|
4.3
|
78.3
|
1.0
|
CD1
|
D:LEU196
|
4.4
|
61.3
|
1.0
|
N
|
D:THR168
|
4.4
|
70.7
|
1.0
|
CA
|
D:ALA167
|
4.4
|
66.7
|
1.0
|
CG
|
D:LEU196
|
4.5
|
61.6
|
1.0
|
HB2
|
D:ALA167
|
4.5
|
79.8
|
1.0
|
HD11
|
D:LEU196
|
4.5
|
79.7
|
1.0
|
CG1
|
D:VAL203
|
4.5
|
76.9
|
1.0
|
HD11
|
D:LEU183
|
4.5
|
98.5
|
1.0
|
HB1
|
D:ALA167
|
4.6
|
79.8
|
1.0
|
CD2
|
D:LEU180
|
4.6
|
73.8
|
1.0
|
C
|
D:ALA167
|
4.6
|
66.3
|
1.0
|
HA
|
D:GLN166
|
4.6
|
76.4
|
1.0
|
HD23
|
D:LEU180
|
4.6
|
93.0
|
1.0
|
HD22
|
D:LEU180
|
4.7
|
93.0
|
1.0
|
HB
|
D:THR198
|
4.7
|
74.3
|
1.0
|
HD11
|
D:ILE207
|
4.7
|
0.1
|
1.0
|
HG13
|
D:VAL203
|
4.7
|
86.8
|
1.0
|
O
|
D:ILE197
|
4.7
|
57.4
|
1.0
|
HD23
|
D:LEU196
|
4.8
|
80.0
|
1.0
|
CB
|
D:THR168
|
4.8
|
71.9
|
1.0
|
HD21
|
D:LEU196
|
4.8
|
80.0
|
1.0
|
HG12
|
D:VAL203
|
4.8
|
86.8
|
1.0
|
HG21
|
D:VAL203
|
4.8
|
84.2
|
1.0
|
HD13
|
D:LEU183
|
4.9
|
98.5
|
1.0
|
H
|
D:GLN166
|
5.0
|
75.1
|
1.0
|
C
|
D:GLN166
|
5.0
|
62.3
|
1.0
|
|
Reference:
P.T.Nguyen,
J.Y.Lai,
A.T.Lee,
J.T.Kaiser,
D.C.Rees.
Noncanonical Role For the Binding Protein in Substrate Uptake By the Metni Methionine Atp Binding Cassette (Abc) Transporter. Proc. Natl. Acad. Sci. V. 115 10596 2018U.S.A..
ISSN: ESSN 1091-6490
PubMed: 30352853
DOI: 10.1073/PNAS.1811003115
Page generated: Sun Aug 11 07:16:26 2024
|