Sodium in PDB 4b5p: Crystal Structure of Human Alpha Tubulin Acetyltransferase Catalytic Domain Q58A Variant
Enzymatic activity of Crystal Structure of Human Alpha Tubulin Acetyltransferase Catalytic Domain Q58A Variant
All present enzymatic activity of Crystal Structure of Human Alpha Tubulin Acetyltransferase Catalytic Domain Q58A Variant:
2.3.1.108;
Protein crystallography data
The structure of Crystal Structure of Human Alpha Tubulin Acetyltransferase Catalytic Domain Q58A Variant, PDB code: 4b5p
was solved by
M.Taschner,
M.Vetter,
E.Lorentzen,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
39.669 /
1.60
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
36.760,
110.870,
113.580,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
18.49 /
22.16
|
Sodium Binding Sites:
The binding sites of Sodium atom in the Crystal Structure of Human Alpha Tubulin Acetyltransferase Catalytic Domain Q58A Variant
(pdb code 4b5p). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the
Crystal Structure of Human Alpha Tubulin Acetyltransferase Catalytic Domain Q58A Variant, PDB code: 4b5p:
Jump to Sodium binding site number:
1;
2;
Sodium binding site 1 out
of 2 in 4b5p
Go back to
Sodium Binding Sites List in 4b5p
Sodium binding site 1 out
of 2 in the Crystal Structure of Human Alpha Tubulin Acetyltransferase Catalytic Domain Q58A Variant
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 1 of Crystal Structure of Human Alpha Tubulin Acetyltransferase Catalytic Domain Q58A Variant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Na401
b:20.2
occ:1.00
|
HE22
|
A:GLN131
|
2.4
|
22.5
|
1.0
|
HZ3
|
A:LYS162
|
2.7
|
22.2
|
1.0
|
HG3
|
A:GLU128
|
2.9
|
25.6
|
1.0
|
HZ2
|
B:LYS162
|
2.9
|
24.8
|
1.0
|
NA
|
B:NA401
|
2.9
|
20.8
|
1.0
|
HB2
|
A:ALA57
|
2.9
|
21.8
|
1.0
|
H71
|
A:ACO1197
|
3.0
|
23.4
|
1.0
|
O
|
A:HOH2059
|
3.2
|
20.7
|
1.0
|
NE2
|
A:GLN131
|
3.2
|
18.8
|
1.0
|
HA
|
A:ALA57
|
3.3
|
23.4
|
1.0
|
NZ
|
A:LYS162
|
3.3
|
18.5
|
1.0
|
OE2
|
A:GLU128
|
3.3
|
23.1
|
1.0
|
HZ1
|
A:LYS162
|
3.4
|
22.2
|
1.0
|
HZ2
|
A:LYS162
|
3.4
|
22.2
|
1.0
|
HZ3
|
B:LYS162
|
3.4
|
24.8
|
1.0
|
H72
|
A:ACO1197
|
3.5
|
23.4
|
1.0
|
CG
|
A:GLU128
|
3.5
|
21.4
|
1.0
|
NZ
|
B:LYS162
|
3.6
|
20.7
|
1.0
|
HG2
|
A:GLU128
|
3.6
|
25.6
|
1.0
|
CB
|
A:ALA57
|
3.6
|
18.1
|
1.0
|
C7P
|
A:ACO1197
|
3.7
|
19.5
|
1.0
|
O
|
A:ALA57
|
3.7
|
23.0
|
1.0
|
HE21
|
A:GLN131
|
3.8
|
22.5
|
1.0
|
CD
|
A:GLU128
|
3.8
|
25.9
|
1.0
|
O
|
A:HOH2057
|
3.8
|
19.8
|
1.0
|
HB3
|
A:ALA57
|
3.8
|
21.8
|
1.0
|
CA
|
A:ALA57
|
3.8
|
19.5
|
1.0
|
OE1
|
A:GLN131
|
3.9
|
21.8
|
1.0
|
HZ1
|
B:LYS162
|
4.0
|
24.8
|
1.0
|
CD
|
A:GLN131
|
4.0
|
17.2
|
1.0
|
HG3
|
B:GLU128
|
4.1
|
27.4
|
1.0
|
HG2
|
B:GLU128
|
4.1
|
27.4
|
1.0
|
C
|
A:ALA57
|
4.2
|
20.6
|
1.0
|
HE1
|
A:TYR125
|
4.4
|
25.0
|
1.0
|
HB1
|
A:ALA57
|
4.5
|
21.8
|
1.0
|
N8P
|
A:ACO1197
|
4.5
|
19.3
|
1.0
|
H62
|
A:ACO1197
|
4.5
|
22.5
|
1.0
|
CG
|
B:GLU128
|
4.5
|
22.8
|
1.0
|
HA
|
A:GLU128
|
4.6
|
24.0
|
1.0
|
HE3
|
B:LYS162
|
4.6
|
21.4
|
1.0
|
HD2
|
A:LYS162
|
4.7
|
23.8
|
1.0
|
CE
|
A:LYS162
|
4.7
|
19.8
|
1.0
|
CE
|
B:LYS162
|
4.7
|
17.8
|
1.0
|
C6P
|
A:ACO1197
|
4.7
|
18.8
|
1.0
|
HE22
|
B:GLN131
|
4.8
|
22.3
|
1.0
|
HN8
|
A:ACO1197
|
4.8
|
23.2
|
1.0
|
O
|
B:ALA57
|
4.9
|
21.8
|
1.0
|
CB
|
A:GLU128
|
4.9
|
22.3
|
1.0
|
OE1
|
A:GLU128
|
4.9
|
21.8
|
1.0
|
HA
|
B:ALA57
|
4.9
|
22.6
|
1.0
|
HE3
|
A:LYS162
|
4.9
|
23.8
|
1.0
|
OE2
|
B:GLU128
|
4.9
|
24.5
|
1.0
|
|
Sodium binding site 2 out
of 2 in 4b5p
Go back to
Sodium Binding Sites List in 4b5p
Sodium binding site 2 out
of 2 in the Crystal Structure of Human Alpha Tubulin Acetyltransferase Catalytic Domain Q58A Variant
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 2 of Crystal Structure of Human Alpha Tubulin Acetyltransferase Catalytic Domain Q58A Variant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Na401
b:20.8
occ:1.00
|
HE22
|
B:GLN131
|
2.4
|
22.3
|
1.0
|
HZ3
|
B:LYS162
|
2.7
|
24.8
|
1.0
|
H71
|
B:ACO1197
|
2.9
|
21.7
|
1.0
|
NA
|
A:NA401
|
2.9
|
20.2
|
1.0
|
HB2
|
B:ALA57
|
2.9
|
25.9
|
1.0
|
HG3
|
B:GLU128
|
2.9
|
27.4
|
1.0
|
HZ2
|
A:LYS162
|
2.9
|
22.2
|
1.0
|
O
|
A:HOH2057
|
3.1
|
19.8
|
1.0
|
NE2
|
B:GLN131
|
3.2
|
18.6
|
1.0
|
NZ
|
B:LYS162
|
3.3
|
20.7
|
1.0
|
HA
|
B:ALA57
|
3.4
|
22.6
|
1.0
|
OE2
|
B:GLU128
|
3.4
|
24.5
|
1.0
|
HZ2
|
B:LYS162
|
3.4
|
24.8
|
1.0
|
HZ1
|
B:LYS162
|
3.4
|
24.8
|
1.0
|
HZ3
|
A:LYS162
|
3.4
|
22.2
|
1.0
|
H72
|
B:ACO1197
|
3.5
|
21.7
|
1.0
|
NZ
|
A:LYS162
|
3.6
|
18.5
|
1.0
|
C7P
|
B:ACO1197
|
3.6
|
18.1
|
1.0
|
CB
|
B:ALA57
|
3.7
|
21.6
|
1.0
|
CG
|
B:GLU128
|
3.7
|
22.8
|
1.0
|
O
|
B:ALA57
|
3.7
|
21.8
|
1.0
|
HE21
|
B:GLN131
|
3.8
|
22.3
|
1.0
|
O
|
A:HOH2059
|
3.8
|
20.7
|
1.0
|
HG2
|
B:GLU128
|
3.8
|
27.4
|
1.0
|
HB3
|
B:ALA57
|
3.8
|
25.9
|
1.0
|
CD
|
B:GLU128
|
3.9
|
23.2
|
1.0
|
OE1
|
B:GLN131
|
3.9
|
19.2
|
1.0
|
CA
|
B:ALA57
|
3.9
|
18.9
|
1.0
|
HG2
|
A:GLU128
|
4.0
|
25.6
|
1.0
|
CD
|
B:GLN131
|
4.0
|
19.3
|
1.0
|
HZ1
|
A:LYS162
|
4.0
|
22.2
|
1.0
|
HG3
|
A:GLU128
|
4.1
|
25.6
|
1.0
|
C
|
B:ALA57
|
4.2
|
19.4
|
1.0
|
HE1
|
B:TYR125
|
4.3
|
25.6
|
0.1
|
HE1
|
B:TYR125
|
4.4
|
24.6
|
0.9
|
HB1
|
B:ALA57
|
4.5
|
25.9
|
1.0
|
N8P
|
B:ACO1197
|
4.5
|
18.5
|
1.0
|
CG
|
A:GLU128
|
4.5
|
21.4
|
1.0
|
H62
|
B:ACO1197
|
4.5
|
24.5
|
1.0
|
HE3
|
A:LYS162
|
4.6
|
23.8
|
1.0
|
HA
|
B:GLU128
|
4.7
|
23.6
|
1.0
|
CE
|
B:LYS162
|
4.7
|
17.8
|
1.0
|
HD2
|
B:LYS162
|
4.7
|
20.1
|
1.0
|
C6P
|
B:ACO1197
|
4.7
|
20.4
|
1.0
|
CE
|
A:LYS162
|
4.7
|
19.8
|
1.0
|
HE22
|
A:GLN131
|
4.8
|
22.5
|
1.0
|
HN8
|
B:ACO1197
|
4.8
|
22.2
|
1.0
|
HA
|
A:ALA57
|
4.8
|
23.4
|
1.0
|
O
|
A:ALA57
|
4.8
|
23.0
|
1.0
|
HE3
|
B:LYS162
|
4.9
|
21.4
|
1.0
|
OE2
|
A:GLU128
|
4.9
|
23.1
|
1.0
|
OE1
|
B:GLU128
|
5.0
|
22.3
|
1.0
|
CB
|
B:GLU128
|
5.0
|
21.9
|
1.0
|
|
Reference:
M.Taschner,
M.Vetter,
E.Lorentzen.
Atomic Resolution Structure of Human Alpha-Tubulin Acetyltransferase Bound to Acetyl-Coa. Proc.Natl.Acad.Sci.Usa V. 109 19649 2012.
ISSN: ISSN 0027-8424
PubMed: 23071318
DOI: 10.1073/PNAS.1209343109
Page generated: Mon Oct 7 14:27:43 2024
|