Chlorine in PDB 6hb1: Structure of HGH1, Crystal Form I
Protein crystallography data
The structure of Structure of HGH1, Crystal Form I, PDB code: 6hb1
was solved by
L.Moenkemeyer,
C.L.Klaips,
D.Balchin,
R.Koerner,
F.U.Hartl,
A.Bracher,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
29.30 /
2.33
|
Space group
|
P 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
80.207,
86.427,
88.368,
118.48,
105.80,
99.15
|
R / Rfree (%)
|
17.7 /
22.6
|
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Structure of HGH1, Crystal Form I
(pdb code 6hb1). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the
Structure of HGH1, Crystal Form I, PDB code: 6hb1:
Jump to Chlorine binding site number:
1;
2;
3;
Chlorine binding site 1 out
of 3 in 6hb1
Go back to
Chlorine Binding Sites List in 6hb1
Chlorine binding site 1 out
of 3 in the Structure of HGH1, Crystal Form I
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 1 of Structure of HGH1, Crystal Form I within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cl401
b:0.3
occ:1.00
|
H
|
A:VAL226
|
2.6
|
37.8
|
1.0
|
HD21
|
D:ASN26
|
2.6
|
48.4
|
1.0
|
HG23
|
A:VAL226
|
2.9
|
36.4
|
1.0
|
HA
|
A:ALA224
|
2.9
|
62.4
|
1.0
|
H
|
A:LYS225
|
3.0
|
34.3
|
1.0
|
O
|
A:HOH572
|
3.1
|
53.0
|
1.0
|
HB
|
A:VAL226
|
3.3
|
51.4
|
1.0
|
N
|
A:LYS225
|
3.3
|
28.6
|
1.0
|
N
|
A:VAL226
|
3.4
|
31.5
|
1.0
|
ND2
|
D:ASN26
|
3.4
|
40.4
|
1.0
|
HG23
|
D:ILE22
|
3.4
|
49.0
|
1.0
|
HB3
|
A:LYS225
|
3.6
|
51.6
|
1.0
|
CG2
|
A:VAL226
|
3.6
|
30.3
|
1.0
|
CA
|
A:ALA224
|
3.7
|
52.0
|
1.0
|
C
|
A:ALA224
|
3.8
|
51.6
|
1.0
|
HG21
|
A:VAL226
|
3.8
|
36.4
|
1.0
|
CB
|
A:VAL226
|
3.8
|
42.8
|
1.0
|
HD22
|
A:ASN181
|
3.9
|
56.2
|
1.0
|
OD1
|
D:ASN26
|
3.9
|
49.3
|
1.0
|
HD22
|
D:ASN26
|
4.0
|
48.4
|
1.0
|
CG
|
D:ASN26
|
4.1
|
41.2
|
1.0
|
HB1
|
A:ALA224
|
4.1
|
60.2
|
1.0
|
CA
|
A:LYS225
|
4.2
|
45.5
|
1.0
|
CG2
|
D:ILE22
|
4.2
|
40.8
|
1.0
|
HG21
|
D:ILE22
|
4.2
|
49.0
|
1.0
|
CA
|
A:VAL226
|
4.2
|
38.2
|
1.0
|
C
|
A:LYS225
|
4.3
|
47.2
|
1.0
|
ND2
|
A:ASN181
|
4.3
|
46.9
|
1.0
|
CB
|
A:LYS225
|
4.3
|
43.0
|
1.0
|
HD21
|
A:ASN181
|
4.4
|
56.2
|
1.0
|
HG22
|
D:ILE22
|
4.4
|
49.0
|
1.0
|
HG22
|
A:VAL226
|
4.4
|
36.4
|
1.0
|
H
|
A:ARG227
|
4.4
|
41.7
|
1.0
|
CB
|
A:ALA224
|
4.5
|
50.2
|
1.0
|
HB2
|
A:LYS225
|
4.6
|
51.6
|
1.0
|
O
|
A:ALA224
|
4.7
|
29.9
|
1.0
|
O
|
A:ASP223
|
4.7
|
50.3
|
1.0
|
HB2
|
A:ALA224
|
4.8
|
60.2
|
1.0
|
N
|
A:ALA224
|
4.8
|
41.3
|
1.0
|
HA
|
A:VAL226
|
4.9
|
45.8
|
1.0
|
HB3
|
A:ASN181
|
4.9
|
37.6
|
1.0
|
|
Chlorine binding site 2 out
of 3 in 6hb1
Go back to
Chlorine Binding Sites List in 6hb1
Chlorine binding site 2 out
of 3 in the Structure of HGH1, Crystal Form I
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 2 of Structure of HGH1, Crystal Form I within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Cl401
b:0.3
occ:1.00
|
HD21
|
B:ASN26
|
2.4
|
53.4
|
1.0
|
H
|
C:VAL226
|
2.6
|
44.5
|
1.0
|
HG23
|
C:VAL226
|
2.9
|
37.5
|
1.0
|
HA
|
C:ALA224
|
3.0
|
46.8
|
1.0
|
H
|
C:LYS225
|
3.1
|
42.1
|
1.0
|
HG23
|
B:ILE22
|
3.2
|
54.6
|
1.0
|
ND2
|
B:ASN26
|
3.2
|
44.5
|
1.0
|
HB
|
C:VAL226
|
3.3
|
37.3
|
1.0
|
O
|
B:HOH448
|
3.3
|
42.9
|
1.0
|
N
|
C:LYS225
|
3.5
|
35.1
|
1.0
|
N
|
C:VAL226
|
3.5
|
37.1
|
1.0
|
CG2
|
C:VAL226
|
3.6
|
31.2
|
1.0
|
HB3
|
C:LYS225
|
3.7
|
59.1
|
1.0
|
CA
|
C:ALA224
|
3.8
|
39.0
|
1.0
|
HG21
|
C:VAL226
|
3.8
|
37.5
|
1.0
|
OD1
|
B:ASN26
|
3.8
|
45.4
|
1.0
|
HD22
|
B:ASN26
|
3.8
|
53.4
|
1.0
|
C
|
C:ALA224
|
3.8
|
37.8
|
1.0
|
CB
|
C:VAL226
|
3.8
|
31.1
|
1.0
|
HD22
|
C:ASN181
|
3.9
|
55.2
|
1.0
|
CG
|
B:ASN26
|
3.9
|
62.7
|
1.0
|
CG2
|
B:ILE22
|
4.0
|
45.5
|
1.0
|
HG21
|
B:ILE22
|
4.0
|
54.6
|
1.0
|
HB1
|
C:ALA224
|
4.2
|
69.6
|
1.0
|
HG22
|
B:ILE22
|
4.2
|
54.6
|
1.0
|
CA
|
C:LYS225
|
4.3
|
50.0
|
1.0
|
CA
|
C:VAL226
|
4.3
|
46.1
|
1.0
|
ND2
|
C:ASN181
|
4.3
|
46.0
|
1.0
|
C
|
C:LYS225
|
4.4
|
40.9
|
1.0
|
CB
|
C:LYS225
|
4.4
|
49.3
|
1.0
|
HG22
|
C:VAL226
|
4.5
|
37.5
|
1.0
|
H
|
C:ARG227
|
4.5
|
47.9
|
1.0
|
HD21
|
C:ASN181
|
4.5
|
55.2
|
1.0
|
CB
|
C:ALA224
|
4.5
|
58.0
|
1.0
|
HB2
|
C:LYS225
|
4.7
|
59.1
|
1.0
|
O
|
C:ALA224
|
4.7
|
32.1
|
1.0
|
O
|
C:ASP223
|
4.7
|
53.9
|
1.0
|
HB3
|
C:ASN181
|
4.8
|
39.1
|
1.0
|
HG12
|
B:ILE22
|
4.8
|
68.5
|
1.0
|
HB2
|
C:ALA224
|
4.8
|
69.6
|
1.0
|
N
|
C:ALA224
|
4.8
|
55.7
|
1.0
|
HA
|
C:VAL226
|
4.9
|
55.3
|
1.0
|
|
Chlorine binding site 3 out
of 3 in 6hb1
Go back to
Chlorine Binding Sites List in 6hb1
Chlorine binding site 3 out
of 3 in the Structure of HGH1, Crystal Form I
Mono view
Stereo pair view
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 3 of Structure of HGH1, Crystal Form I within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Cl401
b:36.2
occ:1.00
|
HD21
|
D:ASN83
|
2.4
|
55.0
|
1.0
|
HE2
|
D:LYS79
|
2.9
|
69.4
|
1.0
|
ND2
|
D:ASN83
|
3.2
|
45.8
|
1.0
|
HZ3
|
D:LYS79
|
3.4
|
74.6
|
1.0
|
HZ1
|
D:LYS79
|
3.5
|
74.6
|
1.0
|
HG3
|
D:LYS79
|
3.6
|
50.1
|
1.0
|
HD22
|
D:ASN83
|
3.6
|
55.0
|
1.0
|
CE
|
D:LYS79
|
3.7
|
57.8
|
1.0
|
NZ
|
D:LYS79
|
3.7
|
62.1
|
1.0
|
HG2
|
D:LYS79
|
3.9
|
50.1
|
1.0
|
HD23
|
D:LEU80
|
4.0
|
48.6
|
1.0
|
CG
|
D:LYS79
|
4.1
|
41.8
|
1.0
|
CG
|
D:ASN83
|
4.2
|
52.0
|
1.0
|
OD1
|
D:ASN83
|
4.3
|
42.8
|
1.0
|
HE3
|
D:LYS79
|
4.3
|
69.4
|
1.0
|
HD21
|
D:LEU80
|
4.4
|
48.6
|
1.0
|
CD
|
D:LYS79
|
4.5
|
61.7
|
1.0
|
HZ2
|
D:LYS79
|
4.6
|
74.6
|
1.0
|
CD2
|
D:LEU80
|
4.6
|
40.5
|
1.0
|
HD22
|
D:LEU80
|
4.9
|
48.6
|
1.0
|
HD2
|
D:LYS79
|
5.0
|
74.1
|
1.0
|
|
Reference:
L.Monkemeyer,
C.L.Klaips,
D.Balchin,
R.Korner,
F.U.Hartl,
A.Bracher.
Chaperone Function of HGH1 in the Biogenesis of Eukaryotic Elongation Factor 2. Mol.Cell V. 74 88 2019.
ISSN: ISSN 1097-2765
PubMed: 30876804
DOI: 10.1016/J.MOLCEL.2019.01.034
Page generated: Sun Jul 28 00:43:10 2024
|