Zinc in PDB 6o7g: Solution Structure of MLL4 PHD6 Domain in Complex with Histone H4K16AC Peptide
Enzymatic activity of Solution Structure of MLL4 PHD6 Domain in Complex with Histone H4K16AC Peptide
All present enzymatic activity of Solution Structure of MLL4 PHD6 Domain in Complex with Histone H4K16AC Peptide:
2.1.1.43;
Zinc Binding Sites:
The binding sites of Zinc atom in the Solution Structure of MLL4 PHD6 Domain in Complex with Histone H4K16AC Peptide
(pdb code 6o7g). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the
Solution Structure of MLL4 PHD6 Domain in Complex with Histone H4K16AC Peptide, PDB code: 6o7g:
Jump to Zinc binding site number:
1;
2;
Zinc binding site 1 out
of 2 in 6o7g
Go back to
Zinc Binding Sites List in 6o7g
Zinc binding site 1 out
of 2 in the Solution Structure of MLL4 PHD6 Domain in Complex with Histone H4K16AC Peptide
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Solution Structure of MLL4 PHD6 Domain in Complex with Histone H4K16AC Peptide within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn1601
b:0.0
occ:1.00
|
ND1
|
B:HIS1531
|
2.3
|
0.0
|
1.0
|
SG
|
B:CYS1507
|
2.4
|
0.0
|
1.0
|
SG
|
B:CYS1534
|
2.4
|
0.0
|
1.0
|
SG
|
B:CYS1510
|
2.4
|
0.0
|
1.0
|
H
|
B:HIS1531
|
3.0
|
0.0
|
1.0
|
HB3
|
B:CYS1534
|
3.2
|
0.0
|
1.0
|
CE1
|
B:HIS1531
|
3.2
|
0.0
|
1.0
|
HB2
|
B:CYS1510
|
3.3
|
0.0
|
1.0
|
HE1
|
B:HIS1531
|
3.3
|
0.0
|
1.0
|
HB2
|
B:HIS1531
|
3.3
|
0.0
|
1.0
|
HB
|
B:ILE1509
|
3.3
|
0.0
|
1.0
|
CB
|
B:CYS1534
|
3.3
|
0.0
|
1.0
|
H
|
B:CYS1510
|
3.3
|
0.0
|
1.0
|
CG
|
B:HIS1531
|
3.4
|
0.0
|
1.0
|
CB
|
B:CYS1507
|
3.4
|
0.0
|
1.0
|
HB3
|
B:CYS1507
|
3.4
|
0.0
|
1.0
|
CB
|
B:CYS1510
|
3.4
|
0.0
|
1.0
|
HB2
|
B:CYS1507
|
3.6
|
0.0
|
1.0
|
HB2
|
B:CYS1534
|
3.7
|
0.0
|
1.0
|
CB
|
B:HIS1531
|
3.8
|
0.0
|
1.0
|
N
|
B:CYS1510
|
3.9
|
0.0
|
1.0
|
N
|
B:HIS1531
|
3.9
|
0.0
|
1.0
|
HB2
|
B:MET1530
|
4.1
|
0.0
|
1.0
|
HB3
|
B:CYS1510
|
4.3
|
0.0
|
1.0
|
CA
|
B:CYS1510
|
4.3
|
0.0
|
1.0
|
H
|
B:CYS1534
|
4.3
|
0.0
|
1.0
|
HD13
|
B:ILE1509
|
4.3
|
0.0
|
1.0
|
NE2
|
B:HIS1531
|
4.4
|
0.0
|
1.0
|
CB
|
B:ILE1509
|
4.4
|
0.0
|
1.0
|
HA
|
B:MET1530
|
4.4
|
0.0
|
1.0
|
CA
|
B:HIS1531
|
4.5
|
0.0
|
1.0
|
CD2
|
B:HIS1531
|
4.5
|
0.0
|
1.0
|
H
|
B:ILE1509
|
4.6
|
0.0
|
1.0
|
C
|
B:ILE1509
|
4.7
|
0.0
|
1.0
|
HG13
|
B:ILE1509
|
4.7
|
0.0
|
1.0
|
HA
|
B:CYS1510
|
4.7
|
0.0
|
1.0
|
CA
|
B:CYS1507
|
4.7
|
0.0
|
1.0
|
CA
|
B:CYS1534
|
4.7
|
0.0
|
1.0
|
HB3
|
B:HIS1531
|
4.8
|
0.0
|
1.0
|
N
|
B:CYS1534
|
4.9
|
0.0
|
1.0
|
C
|
B:MET1530
|
4.9
|
0.0
|
1.0
|
CA
|
B:ILE1509
|
5.0
|
0.0
|
1.0
|
CG1
|
B:ILE1509
|
5.0
|
0.0
|
1.0
|
HA
|
B:CYS1507
|
5.0
|
0.0
|
1.0
|
|
Zinc binding site 2 out
of 2 in 6o7g
Go back to
Zinc Binding Sites List in 6o7g
Zinc binding site 2 out
of 2 in the Solution Structure of MLL4 PHD6 Domain in Complex with Histone H4K16AC Peptide
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Solution Structure of MLL4 PHD6 Domain in Complex with Histone H4K16AC Peptide within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn1602
b:0.0
occ:1.00
|
SG
|
B:CYS1556
|
2.4
|
0.0
|
1.0
|
SG
|
B:CYS1526
|
2.4
|
0.0
|
1.0
|
SG
|
B:CYS1553
|
2.5
|
0.0
|
1.0
|
SG
|
B:CYS1523
|
2.5
|
0.0
|
1.0
|
H
|
B:CYS1553
|
2.8
|
0.0
|
1.0
|
HB2
|
B:CYS1526
|
3.0
|
0.0
|
1.0
|
HB2
|
B:CYS1556
|
3.1
|
0.0
|
1.0
|
H
|
B:CYS1526
|
3.2
|
0.0
|
1.0
|
HB3
|
B:HIS1525
|
3.3
|
0.0
|
1.0
|
CB
|
B:CYS1526
|
3.3
|
0.0
|
1.0
|
CB
|
B:CYS1556
|
3.3
|
0.0
|
1.0
|
HB3
|
B:CYS1553
|
3.5
|
0.0
|
1.0
|
CB
|
B:CYS1523
|
3.5
|
0.0
|
1.0
|
CB
|
B:CYS1553
|
3.5
|
0.0
|
1.0
|
HB2
|
B:CYS1523
|
3.5
|
0.0
|
1.0
|
HB3
|
B:CYS1523
|
3.6
|
0.0
|
1.0
|
N
|
B:CYS1553
|
3.7
|
0.0
|
1.0
|
HD2
|
B:HIS1525
|
3.9
|
0.0
|
1.0
|
HB3
|
B:CYS1556
|
4.0
|
0.0
|
1.0
|
N
|
B:CYS1526
|
4.0
|
0.0
|
1.0
|
H
|
B:CYS1556
|
4.0
|
0.0
|
1.0
|
CA
|
B:CYS1553
|
4.1
|
0.0
|
1.0
|
HB3
|
B:CYS1526
|
4.1
|
0.0
|
1.0
|
HA
|
B:ASP1552
|
4.3
|
0.0
|
1.0
|
CA
|
B:CYS1526
|
4.4
|
0.0
|
1.0
|
H
|
B:HIS1525
|
4.4
|
0.0
|
1.0
|
CB
|
B:HIS1525
|
4.4
|
0.0
|
1.0
|
HB2
|
B:CYS1553
|
4.4
|
0.0
|
1.0
|
N
|
B:CYS1556
|
4.5
|
0.0
|
1.0
|
CA
|
B:CYS1556
|
4.5
|
0.0
|
1.0
|
HB2
|
B:SER1555
|
4.6
|
0.0
|
1.0
|
C
|
B:CYS1553
|
4.7
|
0.0
|
1.0
|
CD2
|
B:HIS1525
|
4.8
|
0.0
|
1.0
|
C
|
B:ASP1552
|
4.8
|
0.0
|
1.0
|
HA
|
B:CYS1556
|
4.8
|
0.0
|
1.0
|
HB3
|
B:ASP1552
|
4.9
|
0.0
|
1.0
|
CA
|
B:CYS1523
|
4.9
|
0.0
|
1.0
|
C
|
B:HIS1525
|
4.9
|
0.0
|
1.0
|
HB2
|
B:HIS1525
|
4.9
|
0.0
|
1.0
|
O
|
B:CYS1553
|
4.9
|
0.0
|
1.0
|
HA
|
B:CYS1526
|
4.9
|
0.0
|
1.0
|
|
Reference:
Y.Zhang,
Y.Jang,
J.E.Lee,
J.Ahn,
L.Xu,
M.R.Holden,
E.M.Cornett,
K.Krajewski,
B.J.Klein,
S.P.Wang,
Y.Dou,
R.G.Roeder,
B.D.Strahl,
S.B.Rothbart,
X.Shi,
K.Ge,
T.G.Kutateladze.
Selective Binding of the PHD6 Finger of MLL4 to Histone H4K16AC Links MLL4 and Mof. Nat Commun V. 10 2314 2019.
ISSN: ESSN 2041-1723
PubMed: 31127101
DOI: 10.1038/S41467-019-10324-8
Page generated: Wed Dec 16 12:25:23 2020
|