Chlorine in PDB 4kha: Structural Basis of Histone H2A-H2B Recognition By the Essential Chaperone Fact
Protein crystallography data
The structure of Structural Basis of Histone H2A-H2B Recognition By the Essential Chaperone Fact, PDB code: 4kha
was solved by
M.Hondele,
F.Halbach,
M.Hassler,
A.G.Ladurner,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
46.70 /
2.35
|
Space group
|
P 43 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
108.421,
108.421,
117.769,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
19.1 /
22.9
|
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Structural Basis of Histone H2A-H2B Recognition By the Essential Chaperone Fact
(pdb code 4kha). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the
Structural Basis of Histone H2A-H2B Recognition By the Essential Chaperone Fact, PDB code: 4kha:
Jump to Chlorine binding site number:
1;
2;
Chlorine binding site 1 out
of 2 in 4kha
Go back to
Chlorine Binding Sites List in 4kha
Chlorine binding site 1 out
of 2 in the Structural Basis of Histone H2A-H2B Recognition By the Essential Chaperone Fact
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 1 of Structural Basis of Histone H2A-H2B Recognition By the Essential Chaperone Fact within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cl1201
b:38.9
occ:1.00
|
H
|
A:ASN916
|
2.5
|
49.1
|
1.0
|
HD22
|
A:ASN916
|
2.6
|
57.0
|
1.0
|
HG
|
A:SER1033
|
2.6
|
50.0
|
1.0
|
H
|
A:ILE1036
|
2.7
|
38.8
|
1.0
|
HG22
|
A:ILE1036
|
3.0
|
47.4
|
1.0
|
HD11
|
A:ILE920
|
3.0
|
47.6
|
1.0
|
HB3
|
A:ALA1035
|
3.1
|
47.7
|
1.0
|
OG
|
A:SER1033
|
3.1
|
41.6
|
1.0
|
HB
|
A:ILE1036
|
3.2
|
65.9
|
1.0
|
HD22
|
A:LEU915
|
3.3
|
56.7
|
1.0
|
HA
|
A:LEU915
|
3.3
|
39.3
|
1.0
|
HB3
|
A:LEU915
|
3.3
|
46.6
|
1.0
|
N
|
A:ASN916
|
3.3
|
41.0
|
1.0
|
ND2
|
A:ASN916
|
3.3
|
47.5
|
1.0
|
HB2
|
A:ASN916
|
3.4
|
46.4
|
1.0
|
N
|
A:ILE1036
|
3.5
|
32.3
|
1.0
|
H
|
A:ALA1035
|
3.6
|
44.4
|
1.0
|
CG2
|
A:ILE1036
|
3.7
|
39.5
|
1.0
|
HB3
|
A:SER1033
|
3.8
|
38.5
|
1.0
|
HD21
|
A:ASN916
|
3.8
|
57.0
|
1.0
|
CB
|
A:ILE1036
|
3.8
|
54.9
|
1.0
|
HG21
|
A:ILE1036
|
3.8
|
47.4
|
1.0
|
CA
|
A:LEU915
|
3.9
|
32.7
|
1.0
|
CD1
|
A:ILE920
|
4.0
|
39.7
|
1.0
|
N
|
A:ALA1035
|
4.0
|
37.0
|
1.0
|
CB
|
A:ALA1035
|
4.0
|
39.7
|
1.0
|
CB
|
A:LEU915
|
4.0
|
38.8
|
1.0
|
CB
|
A:ASN916
|
4.0
|
38.6
|
1.0
|
CB
|
A:SER1033
|
4.0
|
32.1
|
1.0
|
HG13
|
A:ILE920
|
4.1
|
47.6
|
1.0
|
CG
|
A:ASN916
|
4.1
|
41.2
|
1.0
|
CD2
|
A:LEU915
|
4.1
|
47.3
|
1.0
|
C
|
A:LEU915
|
4.1
|
43.5
|
1.0
|
CA
|
A:ASN916
|
4.2
|
37.3
|
1.0
|
CA
|
A:ILE1036
|
4.3
|
41.1
|
1.0
|
HD23
|
A:LEU915
|
4.3
|
56.7
|
1.0
|
HD12
|
A:ILE920
|
4.3
|
47.6
|
1.0
|
CA
|
A:ALA1035
|
4.3
|
36.4
|
1.0
|
HD13
|
A:LEU915
|
4.4
|
43.2
|
1.0
|
HD22
|
A:LEU940
|
4.4
|
55.5
|
1.0
|
C
|
A:ALA1035
|
4.4
|
37.5
|
1.0
|
HG12
|
A:ILE920
|
4.4
|
47.6
|
1.0
|
CG1
|
A:ILE920
|
4.4
|
39.7
|
1.0
|
HB2
|
A:ALA1035
|
4.4
|
47.7
|
1.0
|
O
|
A:SER1033
|
4.5
|
40.6
|
1.0
|
HG23
|
A:ILE1036
|
4.5
|
47.4
|
1.0
|
HD13
|
A:ILE920
|
4.6
|
47.6
|
1.0
|
CG
|
A:LEU915
|
4.6
|
39.1
|
1.0
|
C
|
A:SER1033
|
4.6
|
43.9
|
1.0
|
HB1
|
A:ALA1035
|
4.6
|
47.7
|
1.0
|
HB2
|
A:SER1033
|
4.7
|
38.5
|
1.0
|
C
|
A:TYR1034
|
4.7
|
39.7
|
1.0
|
HA
|
A:ILE1036
|
4.7
|
49.3
|
1.0
|
O
|
A:ASN916
|
4.8
|
39.3
|
1.0
|
HB2
|
A:LEU915
|
4.8
|
46.6
|
1.0
|
C
|
A:ASN916
|
4.8
|
37.6
|
1.0
|
HB3
|
A:LEU940
|
4.9
|
61.0
|
1.0
|
HD21
|
A:LEU915
|
4.9
|
56.7
|
1.0
|
HB3
|
A:ASN916
|
4.9
|
46.4
|
1.0
|
CA
|
A:SER1033
|
5.0
|
41.4
|
1.0
|
|
Chlorine binding site 2 out
of 2 in 4kha
Go back to
Chlorine Binding Sites List in 4kha
Chlorine binding site 2 out
of 2 in the Structural Basis of Histone H2A-H2B Recognition By the Essential Chaperone Fact
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 2 of Structural Basis of Histone H2A-H2B Recognition By the Essential Chaperone Fact within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cl201
b:46.8
occ:1.00
|
H
|
B:GLY28
|
2.5
|
39.8
|
1.0
|
H
|
B:SER18
|
2.9
|
43.7
|
1.0
|
HB
|
B:THR16
|
3.1
|
64.6
|
1.0
|
HB2
|
B:ARG17
|
3.1
|
45.2
|
1.0
|
HB
|
B:VAL27
|
3.2
|
48.1
|
1.0
|
H
|
B:VAL27
|
3.2
|
45.0
|
1.0
|
O
|
B:HOH310
|
3.2
|
41.5
|
1.0
|
O
|
B:HOH307
|
3.3
|
39.6
|
1.0
|
N
|
B:GLY28
|
3.3
|
33.1
|
1.0
|
H
|
B:ARG17
|
3.3
|
48.7
|
1.0
|
OG
|
B:SER18
|
3.4
|
36.8
|
1.0
|
N
|
B:SER18
|
3.5
|
36.4
|
1.0
|
HB2
|
B:SER18
|
3.6
|
46.5
|
1.0
|
HG
|
B:SER18
|
3.6
|
44.2
|
1.0
|
N
|
B:VAL27
|
3.7
|
37.5
|
1.0
|
HA3
|
B:GLY28
|
3.7
|
37.1
|
1.0
|
N
|
B:ARG17
|
3.9
|
40.5
|
1.0
|
CB
|
B:SER18
|
3.9
|
38.8
|
1.0
|
CB
|
B:ARG17
|
4.0
|
37.6
|
1.0
|
CB
|
B:VAL27
|
4.0
|
40.0
|
1.0
|
HA
|
B:PRO26
|
4.0
|
50.9
|
1.0
|
CB
|
B:THR16
|
4.1
|
53.8
|
1.0
|
CA
|
B:GLY28
|
4.1
|
30.9
|
1.0
|
CA
|
B:VAL27
|
4.2
|
43.2
|
1.0
|
C
|
B:VAL27
|
4.2
|
42.0
|
1.0
|
CA
|
B:ARG17
|
4.3
|
42.0
|
1.0
|
CA
|
B:SER18
|
4.3
|
39.5
|
1.0
|
C
|
B:ARG17
|
4.3
|
47.0
|
1.0
|
C
|
B:PRO26
|
4.4
|
37.9
|
1.0
|
HB3
|
B:ARG17
|
4.5
|
45.2
|
1.0
|
HG1
|
B:THR16
|
4.5
|
66.5
|
1.0
|
HA2
|
B:GLY28
|
4.6
|
37.1
|
1.0
|
OG1
|
B:THR16
|
4.6
|
55.4
|
1.0
|
HA
|
B:SER18
|
4.6
|
47.4
|
1.0
|
HG23
|
B:VAL27
|
4.6
|
50.0
|
1.0
|
CA
|
B:PRO26
|
4.7
|
42.5
|
1.0
|
H
|
B:ARG29
|
4.7
|
41.6
|
1.0
|
C
|
B:THR16
|
4.7
|
49.2
|
1.0
|
HG21
|
B:THR16
|
4.7
|
57.8
|
1.0
|
HG12
|
B:VAL27
|
4.8
|
42.8
|
1.0
|
HB3
|
B:SER18
|
4.8
|
46.5
|
1.0
|
HA
|
B:THR16
|
4.8
|
59.4
|
1.0
|
CG2
|
B:THR16
|
4.8
|
48.1
|
1.0
|
HG22
|
B:THR16
|
4.8
|
57.8
|
1.0
|
HG3
|
B:ARG17
|
4.8
|
62.6
|
1.0
|
CA
|
B:THR16
|
4.8
|
49.5
|
1.0
|
CG2
|
B:VAL27
|
4.9
|
41.6
|
1.0
|
HB2
|
B:PRO26
|
4.9
|
43.8
|
1.0
|
CG1
|
B:VAL27
|
5.0
|
35.7
|
1.0
|
|
Reference:
M.Hondele,
T.Stuwe,
M.Hassler,
F.Halbach,
A.Bowman,
E.T.Zhang,
B.Nijmeijer,
C.Kotthoff,
V.Rybin,
S.Amlacher,
E.Hurt,
A.G.Ladurner.
Structural Basis of Histone H2A-H2B Recognition By the Essential Chaperone Fact. Nature V. 499 111 2013.
ISSN: ISSN 0028-0836
PubMed: 23698368
DOI: 10.1038/NATURE12242
Page generated: Sun Jul 21 18:10:02 2024
|