Vanadium in PDB 1lkx: Motor Domain of Myoe, A Class-I Myosin
Protein crystallography data
The structure of Motor Domain of Myoe, A Class-I Myosin, PDB code: 1lkx
was solved by
M.Kollmar,
U.Durrwang,
W.Kliche,
D.J.Manstein,
F.J.Kull,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
50.00 /
3.00
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
51.818,
143.667,
236.050,
90.00,
94.86,
90.00
|
R / Rfree (%)
|
22.8 /
27.3
|
Other elements in 1lkx:
The structure of Motor Domain of Myoe, A Class-I Myosin also contains other interesting chemical elements:
Vanadium Binding Sites:
The binding sites of Vanadium atom in the Motor Domain of Myoe, A Class-I Myosin
(pdb code 1lkx). This binding sites where shown within
5.0 Angstroms radius around Vanadium atom.
In total 4 binding sites of Vanadium where determined in the
Motor Domain of Myoe, A Class-I Myosin, PDB code: 1lkx:
Jump to Vanadium binding site number:
1;
2;
3;
4;
Vanadium binding site 1 out
of 4 in 1lkx
Go back to
Vanadium Binding Sites List in 1lkx
Vanadium binding site 1 out
of 4 in the Motor Domain of Myoe, A Class-I Myosin
Mono view
Stereo pair view
|
A full contact list of Vanadium with other atoms in the V binding
site number 1 of Motor Domain of Myoe, A Class-I Myosin within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:V792
b:30.3
occ:1.00
|
V
|
A:VO4792
|
0.0
|
30.3
|
1.0
|
O2
|
A:VO4792
|
1.7
|
27.9
|
1.0
|
O4
|
A:VO4792
|
1.7
|
33.2
|
1.0
|
O1
|
A:VO4792
|
1.7
|
31.4
|
1.0
|
O3
|
A:VO4792
|
1.7
|
29.9
|
1.0
|
O2B
|
A:ADP791
|
2.0
|
29.4
|
1.0
|
PB
|
A:ADP791
|
3.2
|
29.4
|
1.0
|
O
|
A:HOH805
|
3.5
|
14.3
|
1.0
|
MG
|
A:MG790
|
3.6
|
22.2
|
1.0
|
O1B
|
A:ADP791
|
3.7
|
28.4
|
1.0
|
OG
|
A:SER103
|
3.8
|
41.9
|
1.0
|
O3B
|
A:ADP791
|
3.9
|
28.9
|
1.0
|
N
|
A:SER158
|
3.9
|
33.9
|
1.0
|
NZ
|
A:LYS107
|
3.9
|
27.9
|
1.0
|
CA
|
A:SER103
|
4.0
|
36.1
|
1.0
|
N
|
A:GLY104
|
4.0
|
35.4
|
1.0
|
CA
|
A:SER157
|
4.1
|
35.0
|
1.0
|
ND2
|
A:ASN154
|
4.1
|
38.2
|
1.0
|
OG
|
A:SER157
|
4.2
|
33.2
|
1.0
|
CB
|
A:SER103
|
4.3
|
37.4
|
1.0
|
N
|
A:GLY389
|
4.3
|
46.1
|
1.0
|
O3A
|
A:ADP791
|
4.4
|
28.5
|
1.0
|
C
|
A:SER157
|
4.5
|
34.1
|
1.0
|
C
|
A:SER103
|
4.5
|
36.1
|
1.0
|
O
|
A:SER158
|
4.6
|
34.8
|
1.0
|
CB
|
A:SER157
|
4.6
|
34.3
|
1.0
|
OG
|
A:SER158
|
4.7
|
33.5
|
1.0
|
CB
|
A:SER158
|
4.7
|
34.5
|
1.0
|
CA
|
A:SER158
|
4.8
|
34.2
|
1.0
|
CE
|
A:LYS107
|
4.9
|
25.5
|
1.0
|
CA
|
A:TYR388
|
4.9
|
45.4
|
1.0
|
N
|
A:SER157
|
5.0
|
37.5
|
1.0
|
|
Vanadium binding site 2 out
of 4 in 1lkx
Go back to
Vanadium Binding Sites List in 1lkx
Vanadium binding site 2 out
of 4 in the Motor Domain of Myoe, A Class-I Myosin
Mono view
Stereo pair view
|
A full contact list of Vanadium with other atoms in the V binding
site number 2 of Motor Domain of Myoe, A Class-I Myosin within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:V795
b:43.2
occ:1.00
|
V
|
B:VO4795
|
0.0
|
43.2
|
1.0
|
O1
|
B:VO4795
|
1.7
|
39.9
|
1.0
|
O4
|
B:VO4795
|
1.7
|
41.8
|
1.0
|
O3
|
B:VO4795
|
1.7
|
41.1
|
1.0
|
O2
|
B:VO4795
|
1.7
|
38.8
|
1.0
|
O2B
|
B:ADP794
|
1.9
|
40.1
|
1.0
|
PB
|
B:ADP794
|
3.2
|
40.2
|
1.0
|
MG
|
B:MG793
|
3.5
|
22.8
|
1.0
|
O1B
|
B:ADP794
|
3.7
|
40.9
|
1.0
|
O
|
B:HOH797
|
3.7
|
19.7
|
1.0
|
OG
|
B:SER103
|
3.8
|
39.7
|
1.0
|
N
|
B:SER158
|
3.9
|
38.0
|
1.0
|
NZ
|
B:LYS107
|
3.9
|
34.3
|
1.0
|
CA
|
B:SER103
|
3.9
|
38.8
|
1.0
|
N
|
B:GLY104
|
4.0
|
37.8
|
1.0
|
O3A
|
B:ADP794
|
4.0
|
39.3
|
1.0
|
CA
|
B:SER157
|
4.1
|
38.8
|
1.0
|
ND2
|
B:ASN154
|
4.1
|
44.4
|
1.0
|
OG
|
B:SER157
|
4.2
|
38.3
|
1.0
|
CB
|
B:SER103
|
4.2
|
40.4
|
1.0
|
O3B
|
B:ADP794
|
4.2
|
38.1
|
1.0
|
N
|
B:GLY389
|
4.3
|
49.3
|
1.0
|
C
|
B:SER103
|
4.5
|
38.4
|
1.0
|
C
|
B:SER157
|
4.5
|
38.5
|
1.0
|
O
|
B:SER158
|
4.5
|
39.6
|
1.0
|
CB
|
B:SER157
|
4.6
|
37.9
|
1.0
|
OG
|
B:SER158
|
4.7
|
37.7
|
1.0
|
CB
|
B:SER158
|
4.8
|
37.8
|
1.0
|
CE
|
B:LYS107
|
4.8
|
32.3
|
1.0
|
CA
|
B:SER158
|
4.9
|
37.4
|
1.0
|
CA
|
B:TYR388
|
4.9
|
48.1
|
1.0
|
O
|
B:HOH796
|
4.9
|
14.6
|
1.0
|
N
|
B:SER157
|
5.0
|
40.4
|
1.0
|
|
Vanadium binding site 3 out
of 4 in 1lkx
Go back to
Vanadium Binding Sites List in 1lkx
Vanadium binding site 3 out
of 4 in the Motor Domain of Myoe, A Class-I Myosin
Mono view
Stereo pair view
|
A full contact list of Vanadium with other atoms in the V binding
site number 3 of Motor Domain of Myoe, A Class-I Myosin within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:V892
b:27.7
occ:1.00
|
V
|
C:VO4892
|
0.0
|
27.7
|
1.0
|
O2
|
C:VO4892
|
1.7
|
26.0
|
1.0
|
O1
|
C:VO4892
|
1.7
|
28.6
|
1.0
|
O4
|
C:VO4892
|
1.7
|
27.9
|
1.0
|
O3
|
C:VO4892
|
1.7
|
29.2
|
1.0
|
O2B
|
C:ADP891
|
1.8
|
15.8
|
1.0
|
PB
|
C:ADP891
|
3.2
|
15.0
|
1.0
|
MG
|
C:MG890
|
3.4
|
8.4
|
1.0
|
OG
|
C:SER103
|
3.7
|
45.0
|
1.0
|
N
|
C:GLY104
|
3.8
|
35.3
|
1.0
|
CA
|
C:SER103
|
3.9
|
37.9
|
1.0
|
O3B
|
C:ADP891
|
3.9
|
14.2
|
1.0
|
N
|
C:SER158
|
3.9
|
35.8
|
1.0
|
CA
|
C:SER157
|
4.0
|
36.6
|
1.0
|
ND2
|
C:ASN154
|
4.0
|
41.8
|
1.0
|
NZ
|
C:LYS107
|
4.0
|
29.8
|
1.0
|
O
|
C:HOH909
|
4.0
|
39.4
|
1.0
|
OG
|
C:SER157
|
4.0
|
32.9
|
1.0
|
O1B
|
C:ADP891
|
4.0
|
19.0
|
1.0
|
O3A
|
C:ADP891
|
4.1
|
19.2
|
1.0
|
CB
|
C:SER103
|
4.1
|
40.3
|
1.0
|
N
|
C:GLY389
|
4.2
|
42.9
|
1.0
|
C
|
C:SER103
|
4.3
|
36.5
|
1.0
|
CB
|
C:SER157
|
4.4
|
34.9
|
1.0
|
C
|
C:SER157
|
4.5
|
36.1
|
1.0
|
O
|
C:HOH897
|
4.6
|
28.6
|
1.0
|
O
|
C:SER158
|
4.6
|
33.8
|
1.0
|
CA
|
C:TYR388
|
4.8
|
45.0
|
1.0
|
CA
|
C:GLY104
|
4.8
|
34.0
|
1.0
|
N
|
C:SER157
|
4.9
|
38.6
|
1.0
|
OG
|
C:SER158
|
4.9
|
34.6
|
1.0
|
CB
|
C:SER158
|
4.9
|
35.0
|
1.0
|
CA
|
C:SER158
|
4.9
|
35.0
|
1.0
|
CB
|
C:ASN154
|
4.9
|
42.7
|
1.0
|
CG
|
C:ASN154
|
4.9
|
41.4
|
1.0
|
CA
|
C:GLY389
|
5.0
|
43.8
|
1.0
|
|
Vanadium binding site 4 out
of 4 in 1lkx
Go back to
Vanadium Binding Sites List in 1lkx
Vanadium binding site 4 out
of 4 in the Motor Domain of Myoe, A Class-I Myosin
Mono view
Stereo pair view
|
A full contact list of Vanadium with other atoms in the V binding
site number 4 of Motor Domain of Myoe, A Class-I Myosin within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:V895
b:36.6
occ:1.00
|
V
|
D:VO4895
|
0.0
|
36.6
|
1.0
|
O3B
|
D:ADP894
|
1.7
|
35.8
|
1.0
|
O1
|
D:VO4895
|
1.7
|
38.1
|
1.0
|
O2
|
D:VO4895
|
1.7
|
36.5
|
1.0
|
O4
|
D:VO4895
|
1.7
|
36.5
|
1.0
|
O3
|
D:VO4895
|
1.7
|
35.5
|
1.0
|
PB
|
D:ADP894
|
3.2
|
37.3
|
1.0
|
MG
|
D:MG893
|
3.2
|
5.4
|
1.0
|
O1B
|
D:ADP894
|
3.7
|
39.1
|
1.0
|
NZ
|
D:LYS107
|
3.9
|
29.4
|
1.0
|
OG
|
D:SER103
|
3.9
|
41.0
|
1.0
|
N
|
D:SER158
|
3.9
|
38.0
|
1.0
|
O3A
|
D:ADP894
|
3.9
|
38.1
|
1.0
|
CA
|
D:SER103
|
3.9
|
39.2
|
1.0
|
N
|
D:GLY104
|
4.0
|
36.8
|
1.0
|
O
|
D:HOH906
|
4.0
|
14.2
|
1.0
|
O2B
|
D:ADP894
|
4.1
|
40.6
|
1.0
|
CA
|
D:SER157
|
4.1
|
38.1
|
1.0
|
OG
|
D:SER157
|
4.2
|
35.9
|
1.0
|
ND2
|
D:ASN154
|
4.2
|
43.2
|
1.0
|
N
|
D:GLY389
|
4.2
|
46.6
|
1.0
|
CB
|
D:SER103
|
4.3
|
39.7
|
1.0
|
C
|
D:SER103
|
4.4
|
39.4
|
1.0
|
O
|
D:SER158
|
4.5
|
38.3
|
1.0
|
C
|
D:SER157
|
4.5
|
37.2
|
1.0
|
CB
|
D:SER157
|
4.6
|
37.5
|
1.0
|
CB
|
D:SER158
|
4.7
|
37.2
|
1.0
|
OG
|
D:SER158
|
4.8
|
38.6
|
1.0
|
CA
|
D:TYR388
|
4.8
|
45.7
|
1.0
|
O
|
D:HOH905
|
4.8
|
30.2
|
1.0
|
CE
|
D:LYS107
|
4.8
|
30.7
|
1.0
|
CA
|
D:SER158
|
4.8
|
37.7
|
1.0
|
|
Reference:
M.Kollmar,
U.Durrwang,
W.Kliche,
D.J.Manstein,
F.J.Kull.
Crystal Structure of the Motor Domain of A Class-I Myosin. Embo J. V. 21 2517 2002.
ISSN: ISSN 0261-4189
PubMed: 12032065
DOI: 10.1093/EMBOJ/21.11.2517
Page generated: Fri Oct 11 11:26:12 2024
|