Potassium in PDB 3ezp: Crystal Structure Analysis of Human HDAC8 D101N Variant
Enzymatic activity of Crystal Structure Analysis of Human HDAC8 D101N Variant
All present enzymatic activity of Crystal Structure Analysis of Human HDAC8 D101N Variant:
3.5.1.98;
Protein crystallography data
The structure of Crystal Structure Analysis of Human HDAC8 D101N Variant, PDB code: 3ezp
was solved by
D.P.Dowling,
S.L.Gantt,
S.G.Gattis,
C.A.Fierke,
D.W.Christianon,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
47.23 /
2.65
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
55.310,
85.874,
94.642,
90.00,
93.60,
90.00
|
R / Rfree (%)
|
22.5 /
26.2
|
Other elements in 3ezp:
The structure of Crystal Structure Analysis of Human HDAC8 D101N Variant also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Crystal Structure Analysis of Human HDAC8 D101N Variant
(pdb code 3ezp). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 4 binding sites of Potassium where determined in the
Crystal Structure Analysis of Human HDAC8 D101N Variant, PDB code: 3ezp:
Jump to Potassium binding site number:
1;
2;
3;
4;
Potassium binding site 1 out
of 4 in 3ezp
Go back to
Potassium Binding Sites List in 3ezp
Potassium binding site 1 out
of 4 in the Crystal Structure Analysis of Human HDAC8 D101N Variant
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of Crystal Structure Analysis of Human HDAC8 D101N Variant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K402
b:60.5
occ:1.00
|
O
|
A:HIS180
|
2.6
|
51.5
|
1.0
|
O
|
A:ASP178
|
2.6
|
57.5
|
1.0
|
O
|
A:ASP176
|
2.8
|
58.2
|
1.0
|
OG
|
A:SER199
|
2.9
|
57.6
|
1.0
|
OD1
|
A:ASP176
|
2.9
|
57.8
|
1.0
|
O
|
A:LEU200
|
3.2
|
59.6
|
1.0
|
N
|
A:ASP178
|
3.4
|
56.0
|
1.0
|
CG
|
A:ASP176
|
3.5
|
59.4
|
1.0
|
CB
|
A:HIS201
|
3.5
|
54.8
|
1.0
|
C
|
A:LEU200
|
3.5
|
58.1
|
1.0
|
C
|
A:ASP176
|
3.5
|
57.8
|
1.0
|
C
|
A:ASP178
|
3.5
|
55.4
|
1.0
|
C
|
A:HIS180
|
3.6
|
49.4
|
1.0
|
CB
|
A:ASP176
|
3.7
|
56.6
|
1.0
|
N
|
A:LEU200
|
3.8
|
57.8
|
1.0
|
N
|
A:HIS201
|
3.8
|
57.0
|
1.0
|
CA
|
A:HIS201
|
3.9
|
57.7
|
1.0
|
CA
|
A:ASP178
|
3.9
|
54.9
|
1.0
|
CB
|
A:ASP178
|
4.0
|
55.4
|
1.0
|
CB
|
A:SER199
|
4.1
|
58.1
|
1.0
|
C
|
A:LEU177
|
4.2
|
56.5
|
1.0
|
ND1
|
A:HIS201
|
4.2
|
52.5
|
1.0
|
C
|
A:SER199
|
4.3
|
58.5
|
1.0
|
N
|
A:LEU177
|
4.3
|
56.6
|
1.0
|
CA
|
A:ASP176
|
4.3
|
56.6
|
1.0
|
CG
|
A:HIS201
|
4.3
|
51.2
|
1.0
|
CA
|
A:HIS181
|
4.3
|
52.2
|
1.0
|
N
|
A:HIS180
|
4.3
|
50.0
|
1.0
|
CA
|
A:SER199
|
4.3
|
58.7
|
1.0
|
N
|
A:HIS181
|
4.3
|
51.0
|
1.0
|
CA
|
A:LEU200
|
4.4
|
58.2
|
1.0
|
OD2
|
A:ASP176
|
4.4
|
61.2
|
1.0
|
CA
|
A:LEU177
|
4.4
|
56.1
|
1.0
|
N
|
A:GLY182
|
4.4
|
56.5
|
1.0
|
CA
|
A:HIS180
|
4.5
|
46.5
|
1.0
|
C
|
A:LEU179
|
4.7
|
51.8
|
1.0
|
N
|
A:LEU179
|
4.7
|
52.4
|
1.0
|
C
|
A:HIS181
|
4.8
|
54.6
|
1.0
|
O
|
A:HOH391
|
5.0
|
53.6
|
1.0
|
CE1
|
A:HIS142
|
5.0
|
58.1
|
1.0
|
|
Potassium binding site 2 out
of 4 in 3ezp
Go back to
Potassium Binding Sites List in 3ezp
Potassium binding site 2 out
of 4 in the Crystal Structure Analysis of Human HDAC8 D101N Variant
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of Crystal Structure Analysis of Human HDAC8 D101N Variant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K403
b:66.2
occ:1.00
|
O
|
A:PHE189
|
2.5
|
76.2
|
1.0
|
O
|
A:TYR225
|
2.5
|
76.1
|
1.0
|
O
|
A:HOH396
|
2.6
|
77.1
|
1.0
|
O
|
A:VAL195
|
2.7
|
69.5
|
1.0
|
O
|
A:THR192
|
2.9
|
80.0
|
1.0
|
C
|
A:PHE189
|
3.5
|
76.7
|
1.0
|
C
|
A:TYR225
|
3.6
|
76.4
|
1.0
|
CB
|
A:TYR225
|
3.8
|
81.5
|
1.0
|
C
|
A:VAL195
|
3.8
|
71.0
|
1.0
|
CB
|
A:PHE189
|
3.9
|
75.4
|
1.0
|
OG
|
A:SER226
|
4.0
|
68.4
|
1.0
|
C
|
A:THR192
|
4.1
|
78.8
|
1.0
|
CA
|
A:MET196
|
4.2
|
69.9
|
1.0
|
N
|
A:SER190
|
4.3
|
77.2
|
1.0
|
CA
|
A:SER190
|
4.3
|
78.3
|
1.0
|
CA
|
A:TYR225
|
4.3
|
78.3
|
1.0
|
CA
|
A:PHE189
|
4.3
|
75.3
|
1.0
|
N
|
A:THR197
|
4.4
|
68.2
|
1.0
|
N
|
A:MET196
|
4.5
|
69.9
|
1.0
|
N
|
A:SER226
|
4.5
|
73.8
|
1.0
|
CG2
|
A:THR192
|
4.6
|
79.2
|
1.0
|
C
|
A:SER190
|
4.6
|
78.7
|
1.0
|
N
|
A:THR192
|
4.7
|
78.9
|
1.0
|
O
|
A:GLY222
|
4.8
|
84.0
|
1.0
|
O
|
A:SER190
|
4.8
|
79.0
|
1.0
|
C
|
A:MET196
|
4.8
|
70.2
|
1.0
|
CA
|
A:SER226
|
4.8
|
70.9
|
1.0
|
CG2
|
A:THR197
|
4.8
|
64.1
|
1.0
|
OG1
|
A:THR197
|
4.9
|
65.9
|
1.0
|
CB
|
A:SER226
|
4.9
|
69.5
|
1.0
|
CA
|
A:THR192
|
4.9
|
78.9
|
1.0
|
CA
|
A:VAL195
|
5.0
|
72.4
|
1.0
|
|
Potassium binding site 3 out
of 4 in 3ezp
Go back to
Potassium Binding Sites List in 3ezp
Potassium binding site 3 out
of 4 in the Crystal Structure Analysis of Human HDAC8 D101N Variant
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 3 of Crystal Structure Analysis of Human HDAC8 D101N Variant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K405
b:59.1
occ:1.00
|
O
|
B:ASP178
|
2.5
|
57.1
|
1.0
|
O
|
B:HIS180
|
2.7
|
48.1
|
1.0
|
O
|
B:ASP176
|
2.8
|
58.7
|
1.0
|
OD1
|
B:ASP176
|
3.0
|
54.3
|
1.0
|
OG
|
B:SER199
|
3.0
|
56.9
|
1.0
|
O
|
B:LEU200
|
3.2
|
59.4
|
1.0
|
C
|
B:LEU200
|
3.4
|
57.5
|
1.0
|
N
|
B:ASP178
|
3.4
|
57.9
|
1.0
|
CB
|
B:HIS201
|
3.5
|
54.0
|
1.0
|
C
|
B:ASP178
|
3.5
|
54.9
|
1.0
|
C
|
B:ASP176
|
3.6
|
57.3
|
1.0
|
CG
|
B:ASP176
|
3.6
|
56.2
|
1.0
|
C
|
B:HIS180
|
3.6
|
45.2
|
1.0
|
N
|
B:HIS201
|
3.7
|
56.7
|
1.0
|
N
|
B:LEU200
|
3.7
|
55.6
|
1.0
|
CA
|
B:HIS201
|
3.8
|
55.6
|
1.0
|
CB
|
B:ASP176
|
3.9
|
54.8
|
1.0
|
CA
|
B:ASP178
|
3.9
|
56.0
|
1.0
|
CB
|
B:ASP178
|
4.1
|
56.0
|
1.0
|
C
|
B:LEU177
|
4.1
|
57.7
|
1.0
|
ND1
|
B:HIS201
|
4.2
|
49.8
|
1.0
|
CB
|
B:SER199
|
4.2
|
57.4
|
1.0
|
CA
|
B:LEU200
|
4.2
|
56.9
|
1.0
|
C
|
B:SER199
|
4.2
|
56.0
|
1.0
|
N
|
B:LEU177
|
4.3
|
56.2
|
1.0
|
N
|
B:HIS180
|
4.3
|
45.5
|
1.0
|
CG
|
B:HIS201
|
4.3
|
50.5
|
1.0
|
CA
|
B:LEU177
|
4.3
|
56.6
|
1.0
|
CA
|
B:ASP176
|
4.4
|
56.0
|
1.0
|
N
|
B:HIS181
|
4.4
|
46.3
|
1.0
|
CA
|
B:SER199
|
4.4
|
56.9
|
1.0
|
CA
|
B:HIS181
|
4.4
|
48.4
|
1.0
|
OD2
|
B:ASP176
|
4.5
|
57.3
|
1.0
|
CA
|
B:HIS180
|
4.6
|
42.3
|
1.0
|
N
|
B:GLY182
|
4.6
|
53.1
|
1.0
|
C
|
B:LEU179
|
4.6
|
49.5
|
1.0
|
N
|
B:LEU179
|
4.6
|
51.3
|
1.0
|
C
|
B:HIS181
|
4.9
|
52.2
|
1.0
|
O
|
B:LEU177
|
4.9
|
60.3
|
1.0
|
|
Potassium binding site 4 out
of 4 in 3ezp
Go back to
Potassium Binding Sites List in 3ezp
Potassium binding site 4 out
of 4 in the Crystal Structure Analysis of Human HDAC8 D101N Variant
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 4 of Crystal Structure Analysis of Human HDAC8 D101N Variant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K406
b:61.6
occ:1.00
|
O
|
B:VAL195
|
2.4
|
66.2
|
1.0
|
O
|
B:PHE189
|
2.5
|
74.5
|
1.0
|
O
|
B:TYR225
|
2.7
|
73.7
|
1.0
|
O
|
B:HOH390
|
2.8
|
60.1
|
1.0
|
O
|
B:THR192
|
2.8
|
77.2
|
1.0
|
O
|
B:HOH398
|
3.1
|
62.4
|
1.0
|
C
|
B:PHE189
|
3.5
|
74.3
|
1.0
|
C
|
B:VAL195
|
3.6
|
68.2
|
1.0
|
CB
|
B:PHE189
|
3.7
|
74.2
|
1.0
|
C
|
B:TYR225
|
3.7
|
74.7
|
1.0
|
CB
|
B:TYR225
|
3.8
|
79.9
|
1.0
|
C
|
B:THR192
|
4.0
|
77.8
|
1.0
|
CA
|
B:MET196
|
4.1
|
68.8
|
1.0
|
OG
|
B:SER226
|
4.2
|
68.2
|
1.0
|
CA
|
B:PHE189
|
4.3
|
73.9
|
1.0
|
N
|
B:MET196
|
4.4
|
67.5
|
1.0
|
N
|
B:SER190
|
4.4
|
74.4
|
1.0
|
CG2
|
B:THR192
|
4.4
|
78.3
|
1.0
|
N
|
B:THR197
|
4.4
|
67.1
|
1.0
|
CA
|
B:SER190
|
4.4
|
75.1
|
1.0
|
CA
|
B:TYR225
|
4.4
|
76.6
|
1.0
|
N
|
B:THR192
|
4.7
|
76.4
|
1.0
|
N
|
B:SER226
|
4.7
|
72.4
|
1.0
|
CA
|
B:VAL195
|
4.7
|
69.4
|
1.0
|
C
|
B:SER190
|
4.7
|
74.6
|
1.0
|
C
|
B:MET196
|
4.8
|
69.0
|
1.0
|
CA
|
B:THR192
|
4.8
|
77.1
|
1.0
|
CG2
|
B:THR197
|
4.9
|
63.6
|
1.0
|
N
|
B:VAL195
|
4.9
|
72.0
|
1.0
|
O
|
B:SER190
|
4.9
|
74.7
|
1.0
|
N
|
B:SER193
|
4.9
|
77.3
|
1.0
|
CB
|
B:VAL195
|
4.9
|
69.6
|
1.0
|
O
|
B:GLY222
|
5.0
|
83.1
|
1.0
|
OG1
|
B:THR197
|
5.0
|
60.7
|
1.0
|
|
Reference:
D.P.Dowling,
S.L.Gantt,
S.G.Gattis,
C.A.Fierke,
D.W.Christianson.
Structural Studies of Human Histone Deacetylase 8 and Its Site-Specific Variants Complexed with Substrate and Inhibitors. Biochemistry V. 47 13554 2008.
ISSN: ISSN 0006-2960
PubMed: 19053282
DOI: 10.1021/BI801610C
Page generated: Mon Aug 12 08:13:13 2024
|