Zinc in PDB 5h7r: Structural Basis of the Flanking Zinc-Finger Motifs Crucial For the E3 Ligase Activity of the LNX1 Ring Domain
Protein crystallography data
The structure of Structural Basis of the Flanking Zinc-Finger Motifs Crucial For the E3 Ligase Activity of the LNX1 Ring Domain, PDB code: 5h7r
was solved by
D.Nayak,
J.Sivaraman,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
79.88 /
1.70
|
Space group
|
P 62 2 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
92.375,
92.375,
84.410,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
17.8 /
21.5
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Structural Basis of the Flanking Zinc-Finger Motifs Crucial For the E3 Ligase Activity of the LNX1 Ring Domain
(pdb code 5h7r). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the
Structural Basis of the Flanking Zinc-Finger Motifs Crucial For the E3 Ligase Activity of the LNX1 Ring Domain, PDB code: 5h7r:
Jump to Zinc binding site number:
1;
2;
3;
4;
Zinc binding site 1 out
of 4 in 5h7r
Go back to
Zinc Binding Sites List in 5h7r
Zinc binding site 1 out
of 4 in the Structural Basis of the Flanking Zinc-Finger Motifs Crucial For the E3 Ligase Activity of the LNX1 Ring Domain
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Structural Basis of the Flanking Zinc-Finger Motifs Crucial For the E3 Ligase Activity of the LNX1 Ring Domain within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn201
b:27.0
occ:1.00
|
NE2
|
D:HIS11
|
2.0
|
23.9
|
1.0
|
SG
|
D:CYS4
|
2.3
|
29.8
|
1.0
|
CD2
|
D:HIS17
|
2.3
|
30.1
|
1.0
|
SG
|
D:CYS7
|
2.3
|
23.5
|
1.0
|
NE2
|
D:HIS17
|
2.7
|
30.3
|
1.0
|
CE1
|
D:HIS11
|
2.9
|
33.3
|
1.0
|
CD2
|
D:HIS11
|
3.0
|
25.3
|
1.0
|
CB
|
D:CYS4
|
3.0
|
44.1
|
1.0
|
CG
|
D:HIS17
|
3.2
|
29.6
|
1.0
|
CB
|
D:CYS7
|
3.4
|
23.3
|
1.0
|
CA
|
D:HIS17
|
3.7
|
25.4
|
1.0
|
CE1
|
D:HIS17
|
3.7
|
27.0
|
1.0
|
N
|
D:CYS7
|
3.7
|
19.3
|
1.0
|
CB
|
D:HIS17
|
3.9
|
26.2
|
1.0
|
ND1
|
D:HIS17
|
3.9
|
33.0
|
1.0
|
ND1
|
D:HIS11
|
4.1
|
28.5
|
1.0
|
CA
|
D:CYS7
|
4.1
|
23.5
|
1.0
|
CG
|
D:HIS11
|
4.2
|
30.6
|
1.0
|
N
|
D:HIS17
|
4.4
|
20.1
|
1.0
|
CB
|
D:VAL6
|
4.5
|
27.4
|
1.0
|
CA
|
D:CYS4
|
4.5
|
34.4
|
1.0
|
N
|
D:PHE18
|
4.7
|
22.2
|
1.0
|
C
|
D:VAL6
|
4.7
|
21.5
|
1.0
|
C
|
D:HIS17
|
4.8
|
23.9
|
1.0
|
C
|
D:CYS7
|
4.8
|
23.4
|
1.0
|
CA
|
D:VAL6
|
5.0
|
26.1
|
1.0
|
N
|
D:VAL6
|
5.0
|
29.9
|
1.0
|
C
|
D:CYS4
|
5.0
|
28.4
|
1.0
|
N
|
D:GLY8
|
5.0
|
22.4
|
1.0
|
|
Zinc binding site 2 out
of 4 in 5h7r
Go back to
Zinc Binding Sites List in 5h7r
Zinc binding site 2 out
of 4 in the Structural Basis of the Flanking Zinc-Finger Motifs Crucial For the E3 Ligase Activity of the LNX1 Ring Domain
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Structural Basis of the Flanking Zinc-Finger Motifs Crucial For the E3 Ligase Activity of the LNX1 Ring Domain within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn202
b:22.7
occ:1.00
|
SG
|
D:CYS31
|
2.3
|
21.8
|
1.0
|
SG
|
D:CYS54
|
2.3
|
23.4
|
1.0
|
SG
|
D:CYS34
|
2.3
|
23.2
|
1.0
|
SG
|
D:CYS51
|
2.3
|
21.4
|
1.0
|
CB
|
D:CYS31
|
3.0
|
22.1
|
1.0
|
CB
|
D:CYS51
|
3.2
|
20.5
|
1.0
|
CB
|
D:CYS34
|
3.3
|
26.9
|
1.0
|
CB
|
D:CYS54
|
3.3
|
21.3
|
1.0
|
N
|
D:CYS34
|
3.8
|
28.9
|
1.0
|
N
|
D:CYS51
|
4.0
|
20.2
|
1.0
|
ND2
|
D:ASN16
|
4.1
|
28.4
|
1.0
|
O
|
D:HOH361
|
4.2
|
31.6
|
1.0
|
CA
|
D:CYS34
|
4.2
|
25.3
|
1.0
|
CA
|
D:CYS51
|
4.2
|
18.8
|
1.0
|
CA
|
D:CYS31
|
4.5
|
23.4
|
1.0
|
CA
|
D:CYS54
|
4.7
|
20.7
|
1.0
|
CB
|
D:ILE33
|
4.7
|
28.0
|
1.0
|
C
|
D:ILE33
|
4.9
|
30.4
|
1.0
|
O
|
D:GLN36
|
4.9
|
21.8
|
1.0
|
C
|
D:CYS31
|
4.9
|
24.5
|
1.0
|
C
|
D:CYS34
|
5.0
|
27.3
|
1.0
|
|
Zinc binding site 3 out
of 4 in 5h7r
Go back to
Zinc Binding Sites List in 5h7r
Zinc binding site 3 out
of 4 in the Structural Basis of the Flanking Zinc-Finger Motifs Crucial For the E3 Ligase Activity of the LNX1 Ring Domain
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Structural Basis of the Flanking Zinc-Finger Motifs Crucial For the E3 Ligase Activity of the LNX1 Ring Domain within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn203
b:31.5
occ:1.00
|
NE2
|
D:HIS113
|
2.1
|
18.5
|
1.0
|
SG
|
D:CYS95
|
2.3
|
24.0
|
1.0
|
SG
|
D:CYS101
|
2.4
|
26.8
|
1.0
|
SG
|
D:CYS118
|
2.4
|
36.5
|
1.0
|
CE1
|
D:HIS113
|
3.1
|
26.7
|
1.0
|
CD2
|
D:HIS113
|
3.1
|
20.0
|
1.0
|
CB
|
D:CYS101
|
3.1
|
27.1
|
1.0
|
CB
|
D:CYS118
|
3.3
|
27.1
|
1.0
|
CB
|
D:CYS95
|
3.3
|
23.2
|
1.0
|
CA
|
D:CYS118
|
4.1
|
37.7
|
1.0
|
ND1
|
D:HIS113
|
4.2
|
25.5
|
1.0
|
CG
|
D:HIS113
|
4.2
|
23.7
|
1.0
|
O
|
D:HOH355
|
4.4
|
36.4
|
1.0
|
CB
|
D:GLN103
|
4.4
|
28.6
|
1.0
|
CA
|
D:CYS101
|
4.6
|
25.2
|
1.0
|
CA
|
D:CYS95
|
4.7
|
20.9
|
1.0
|
CE1
|
D:PHE114
|
4.8
|
24.3
|
1.0
|
CD2
|
D:PHE97
|
4.8
|
25.1
|
1.0
|
CD1
|
D:PHE114
|
4.8
|
21.0
|
1.0
|
CB
|
D:PHE97
|
4.9
|
24.9
|
1.0
|
C
|
D:CYS118
|
4.9
|
35.6
|
1.0
|
N
|
D:LYS119
|
5.0
|
39.4
|
1.0
|
|
Zinc binding site 4 out
of 4 in 5h7r
Go back to
Zinc Binding Sites List in 5h7r
Zinc binding site 4 out
of 4 in the Structural Basis of the Flanking Zinc-Finger Motifs Crucial For the E3 Ligase Activity of the LNX1 Ring Domain
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Structural Basis of the Flanking Zinc-Finger Motifs Crucial For the E3 Ligase Activity of the LNX1 Ring Domain within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn204
b:27.3
occ:1.00
|
OD2
|
D:ASP68
|
2.0
|
25.4
|
1.0
|
SG
|
D:CYS65
|
2.2
|
28.5
|
1.0
|
CD2
|
D:HIS48
|
2.3
|
24.5
|
1.0
|
SG
|
D:CYS46
|
2.4
|
28.7
|
1.0
|
CG
|
D:ASP68
|
2.8
|
32.5
|
1.0
|
OD1
|
D:ASP68
|
3.0
|
31.0
|
1.0
|
CB
|
D:CYS65
|
3.2
|
28.5
|
1.0
|
CG
|
D:HIS48
|
3.2
|
24.3
|
1.0
|
NE2
|
D:HIS48
|
3.3
|
28.7
|
1.0
|
CB
|
D:CYS46
|
3.3
|
26.9
|
1.0
|
CB
|
D:HIS48
|
3.7
|
21.9
|
1.0
|
OG1
|
D:THR44
|
4.0
|
25.5
|
1.0
|
CB
|
D:ASP68
|
4.1
|
27.9
|
1.0
|
CE1
|
D:HIS48
|
4.3
|
25.7
|
1.0
|
ND1
|
D:HIS48
|
4.3
|
30.8
|
1.0
|
O
|
D:CYS46
|
4.3
|
30.6
|
1.0
|
N
|
D:ASP68
|
4.4
|
32.6
|
1.0
|
C
|
D:CYS46
|
4.5
|
28.7
|
1.0
|
CA
|
D:CYS46
|
4.5
|
28.5
|
1.0
|
CB
|
D:MET67
|
4.6
|
29.5
|
1.0
|
CA
|
D:CYS65
|
4.6
|
29.6
|
1.0
|
OH
|
D:TYR50
|
4.6
|
31.1
|
1.0
|
N
|
D:HIS48
|
4.7
|
19.9
|
1.0
|
CA
|
D:HIS48
|
4.9
|
20.8
|
1.0
|
CA
|
D:ASP68
|
4.9
|
31.2
|
1.0
|
CB
|
D:THR44
|
5.0
|
22.5
|
1.0
|
|
Reference:
D.Nayak,
J.Sivaraman.
Structure of LNX1:UBC13~Ubiquitin Complex Reveals the Role of Additional Motifs For the E3 Ligase Activity of LNX1. J. Mol. Biol. V. 430 1173 2018.
ISSN: ESSN 1089-8638
PubMed: 29496391
DOI: 10.1016/J.JMB.2018.02.016
Page generated: Sun Oct 27 17:21:42 2024
|