Zinc in PDB 8or2: CAND1-CUL1-RBX1-DCNL1
Enzymatic activity of CAND1-CUL1-RBX1-DCNL1
Zinc Binding Sites:
The binding sites of Zinc atom in the CAND1-CUL1-RBX1-DCNL1
(pdb code 8or2). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the
CAND1-CUL1-RBX1-DCNL1, PDB code: 8or2:
Jump to Zinc binding site number:
1;
2;
3;
Zinc binding site 1 out
of 3 in 8or2
Go back to
Zinc Binding Sites List in 8or2
Zinc binding site 1 out
of 3 in the CAND1-CUL1-RBX1-DCNL1
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of CAND1-CUL1-RBX1-DCNL1 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn4001
b:69.5
occ:1.00
|
ND1
|
B:HIS80
|
2.3
|
53.7
|
1.0
|
SG
|
B:CYS45
|
2.3
|
56.5
|
1.0
|
SG
|
B:CYS83
|
2.3
|
54.5
|
1.0
|
CB
|
B:HIS80
|
2.7
|
53.7
|
1.0
|
CG
|
B:HIS80
|
2.8
|
53.7
|
1.0
|
CB
|
B:CYS83
|
2.8
|
54.5
|
1.0
|
SG
|
B:CYS42
|
3.4
|
54.7
|
1.0
|
CE1
|
B:HIS80
|
3.4
|
53.7
|
1.0
|
CB
|
B:CYS45
|
3.5
|
56.5
|
1.0
|
N
|
B:HIS80
|
3.5
|
53.7
|
1.0
|
CA
|
B:HIS80
|
3.7
|
53.7
|
1.0
|
CD2
|
B:HIS80
|
4.0
|
53.7
|
1.0
|
N
|
B:CYS45
|
4.0
|
56.5
|
1.0
|
CA
|
B:CYS83
|
4.3
|
54.5
|
1.0
|
NE2
|
B:HIS80
|
4.3
|
53.7
|
1.0
|
CB
|
B:CYS42
|
4.3
|
54.7
|
1.0
|
CA
|
B:CYS45
|
4.4
|
56.5
|
1.0
|
CB
|
B:ILE44
|
4.4
|
53.9
|
1.0
|
C
|
B:HIS80
|
4.5
|
53.7
|
1.0
|
N
|
B:CYS83
|
4.6
|
54.5
|
1.0
|
O
|
B:HIS80
|
4.6
|
53.7
|
1.0
|
C
|
B:PHE79
|
4.7
|
52.8
|
1.0
|
CG2
|
B:ILE44
|
5.0
|
53.9
|
1.0
|
C
|
B:ILE44
|
5.0
|
53.9
|
1.0
|
|
Zinc binding site 2 out
of 3 in 8or2
Go back to
Zinc Binding Sites List in 8or2
Zinc binding site 2 out
of 3 in the CAND1-CUL1-RBX1-DCNL1
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of CAND1-CUL1-RBX1-DCNL1 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn4002
b:63.2
occ:1.00
|
ND1
|
B:HIS77
|
2.3
|
52.3
|
1.0
|
SG
|
B:CYS94
|
2.3
|
53.9
|
1.0
|
SG
|
B:CYS75
|
2.3
|
53.9
|
1.0
|
CE1
|
B:HIS77
|
3.1
|
52.3
|
1.0
|
CB
|
B:CYS94
|
3.2
|
53.9
|
1.0
|
CG
|
B:HIS77
|
3.4
|
52.3
|
1.0
|
OD1
|
B:ASP97
|
3.5
|
55.1
|
1.0
|
CB
|
B:CYS75
|
3.5
|
53.9
|
1.0
|
OD2
|
B:ASP97
|
3.7
|
55.1
|
1.0
|
CG
|
B:ASP97
|
3.8
|
55.1
|
1.0
|
CE3
|
B:TRP101
|
3.8
|
51.7
|
1.0
|
CB
|
B:HIS77
|
3.8
|
52.3
|
1.0
|
CZ3
|
B:TRP101
|
3.8
|
51.7
|
1.0
|
NE2
|
B:HIS77
|
4.3
|
52.3
|
1.0
|
CB
|
B:LEU96
|
4.4
|
54.8
|
1.0
|
CE2
|
B:PHE79
|
4.4
|
52.8
|
1.0
|
CD1
|
B:LEU96
|
4.4
|
54.8
|
1.0
|
CD2
|
B:HIS77
|
4.5
|
52.3
|
1.0
|
CA
|
B:CYS94
|
4.7
|
53.9
|
1.0
|
N
|
B:ASP97
|
4.7
|
55.1
|
1.0
|
CB
|
B:ASP97
|
4.9
|
55.1
|
1.0
|
CA
|
B:CYS75
|
4.9
|
53.9
|
1.0
|
CG
|
B:LEU96
|
4.9
|
54.8
|
1.0
|
|
Zinc binding site 3 out
of 3 in 8or2
Go back to
Zinc Binding Sites List in 8or2
Zinc binding site 3 out
of 3 in the CAND1-CUL1-RBX1-DCNL1
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of CAND1-CUL1-RBX1-DCNL1 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn4003
b:73.0
occ:1.00
|
SG
|
B:CYS56
|
2.3
|
60.3
|
1.0
|
SG
|
B:CYS68
|
2.3
|
55.9
|
1.0
|
SG
|
B:CYS53
|
2.3
|
58.3
|
1.0
|
CB
|
B:CYS68
|
2.5
|
55.9
|
1.0
|
CB
|
B:CYS56
|
3.1
|
60.3
|
1.0
|
CB
|
B:CYS53
|
3.1
|
58.3
|
1.0
|
N
|
B:CYS53
|
3.2
|
58.3
|
1.0
|
CA
|
B:CYS53
|
3.7
|
58.3
|
1.0
|
CA
|
B:CYS68
|
4.0
|
55.9
|
1.0
|
CD2
|
B:HIS82
|
4.3
|
54.5
|
1.0
|
C
|
B:LEU52
|
4.3
|
58.7
|
1.0
|
CA
|
B:CYS56
|
4.3
|
60.3
|
1.0
|
N
|
B:CYS56
|
4.4
|
60.3
|
1.0
|
CA
|
B:LEU52
|
4.5
|
58.7
|
1.0
|
C
|
B:CYS53
|
4.5
|
58.3
|
1.0
|
O
|
B:CYS53
|
4.6
|
58.3
|
1.0
|
C
|
B:CYS68
|
4.7
|
55.9
|
1.0
|
O
|
B:CYS68
|
4.7
|
55.9
|
1.0
|
N
|
B:CYS68
|
4.8
|
55.9
|
1.0
|
CB
|
B:LEU52
|
4.8
|
58.7
|
1.0
|
NE2
|
B:HIS82
|
4.8
|
54.5
|
1.0
|
CG
|
B:HIS82
|
4.9
|
54.5
|
1.0
|
|
Reference:
M.Shaaban,
J.A.Clapperton,
S.Ding,
S.Kunzelmann,
M.E.Maeots,
S.L.Maslen,
J.M.Skehel,
R.I.Enchev.
Structural and Mechanistic Insights Into the CAND1-Mediated Scf Substrate Receptor Exchange. Mol.Cell 2023.
ISSN: ISSN 1097-2765
PubMed: 37339624
DOI: 10.1016/J.MOLCEL.2023.05.034
Page generated: Thu Oct 31 08:53:32 2024
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