Zinc in PDB 9qlm: Solution Structure of the TAF3-Phd Bound to A H3K4ME3Q5SER Histone Tail Peptide with A Serotonylated Glutamine
Zinc Binding Sites:
The binding sites of Zinc atom in the Solution Structure of the TAF3-Phd Bound to A H3K4ME3Q5SER Histone Tail Peptide with A Serotonylated Glutamine
(pdb code 9qlm). 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 the TAF3-Phd Bound to A H3K4ME3Q5SER Histone Tail Peptide with A Serotonylated Glutamine, PDB code: 9qlm:
Jump to Zinc binding site number:
1;
2;
Zinc binding site 1 out
of 2 in 9qlm
Go back to
Zinc Binding Sites List in 9qlm
Zinc binding site 1 out
of 2 in the Solution Structure of the TAF3-Phd Bound to A H3K4ME3Q5SER Histone Tail Peptide with A Serotonylated Glutamine
 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 the TAF3-Phd Bound to A H3K4ME3Q5SER Histone Tail Peptide with A Serotonylated Glutamine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1001
b:15.0
occ:1.00
|
SG
|
A:CYS885
|
2.5
|
15.0
|
1.0
|
SG
|
A:CYS914
|
2.5
|
15.0
|
1.0
|
SG
|
A:CYS888
|
2.7
|
15.0
|
1.0
|
SG
|
A:CYS911
|
2.7
|
15.0
|
1.0
|
HB3
|
A:CYS911
|
2.7
|
15.0
|
1.0
|
H
|
A:CYS888
|
2.8
|
15.0
|
1.0
|
HZ3
|
A:LYS913
|
2.9
|
15.0
|
1.0
|
HB2
|
A:CYS914
|
2.9
|
15.0
|
1.0
|
H
|
A:CYS911
|
2.9
|
15.0
|
1.0
|
HB2
|
A:CYS888
|
3.0
|
15.0
|
1.0
|
HZ2
|
A:LYS913
|
3.1
|
15.0
|
1.0
|
CB
|
A:CYS911
|
3.2
|
15.0
|
1.0
|
HB2
|
A:CYS885
|
3.3
|
15.0
|
1.0
|
CB
|
A:CYS885
|
3.3
|
15.0
|
1.0
|
CB
|
A:CYS914
|
3.3
|
15.0
|
1.0
|
HB3
|
A:CYS885
|
3.3
|
15.0
|
1.0
|
CB
|
A:CYS888
|
3.4
|
15.0
|
1.0
|
HH
|
A:TYR892
|
3.4
|
15.0
|
1.0
|
HB3
|
A:ASP887
|
3.4
|
15.0
|
1.0
|
H
|
A:CYS914
|
3.4
|
15.0
|
1.0
|
NZ
|
A:LYS913
|
3.4
|
15.0
|
1.0
|
N
|
A:CYS888
|
3.7
|
15.0
|
1.0
|
HZ1
|
A:LYS913
|
3.7
|
15.0
|
1.0
|
N
|
A:CYS911
|
3.7
|
15.0
|
1.0
|
HB3
|
A:CYS914
|
4.0
|
15.0
|
1.0
|
CA
|
A:CYS911
|
4.1
|
15.0
|
1.0
|
OH
|
A:TYR892
|
4.1
|
15.0
|
1.0
|
HB2
|
A:CYS911
|
4.1
|
15.0
|
1.0
|
CA
|
A:CYS888
|
4.1
|
15.0
|
1.0
|
HB2
|
A:ASP887
|
4.1
|
15.0
|
1.0
|
HB2
|
A:LYS913
|
4.1
|
15.0
|
1.0
|
N
|
A:CYS914
|
4.2
|
15.0
|
1.0
|
HZ1
|
A:LYS917
|
4.2
|
15.0
|
1.0
|
CB
|
A:ASP887
|
4.2
|
15.0
|
1.0
|
H
|
A:ASP887
|
4.3
|
15.0
|
1.0
|
HB3
|
A:CYS888
|
4.3
|
15.0
|
1.0
|
CA
|
A:CYS914
|
4.4
|
15.0
|
1.0
|
HE1
|
A:TYR892
|
4.4
|
15.0
|
1.0
|
CZ
|
A:TYR892
|
4.5
|
15.0
|
1.0
|
HB3
|
A:PHE910
|
4.5
|
15.0
|
1.0
|
HA
|
A:PHE910
|
4.5
|
15.0
|
1.0
|
H
|
A:LYS913
|
4.6
|
15.0
|
1.0
|
CE1
|
A:TYR892
|
4.6
|
15.0
|
1.0
|
HA
|
A:CYS888
|
4.7
|
15.0
|
1.0
|
C
|
A:ASP887
|
4.7
|
15.0
|
1.0
|
HD1
|
A:PHE910
|
4.8
|
15.0
|
1.0
|
C
|
A:CYS911
|
4.8
|
15.0
|
1.0
|
CA
|
A:CYS885
|
4.8
|
15.0
|
1.0
|
CE
|
A:LYS913
|
4.8
|
15.0
|
1.0
|
HG3
|
A:LYS913
|
4.8
|
15.0
|
1.0
|
O
|
A:CYS911
|
4.8
|
15.0
|
1.0
|
H
|
A:ASP889
|
4.8
|
15.0
|
1.0
|
C
|
A:PHE910
|
4.9
|
15.0
|
1.0
|
CA
|
A:ASP887
|
4.9
|
15.0
|
1.0
|
HE2
|
A:LYS913
|
4.9
|
15.0
|
1.0
|
N
|
A:ASP887
|
5.0
|
15.0
|
1.0
|
HA
|
A:CYS914
|
5.0
|
15.0
|
1.0
|
HA
|
A:CYS911
|
5.0
|
15.0
|
1.0
|
|
Zinc binding site 2 out
of 2 in 9qlm
Go back to
Zinc Binding Sites List in 9qlm
Zinc binding site 2 out
of 2 in the Solution Structure of the TAF3-Phd Bound to A H3K4ME3Q5SER Histone Tail Peptide with A Serotonylated Glutamine
 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 the TAF3-Phd Bound to A H3K4ME3Q5SER Histone Tail Peptide with A Serotonylated Glutamine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1002
b:15.0
occ:1.00
|
HB2
|
A:HIS893
|
2.0
|
15.0
|
1.0
|
ND1
|
A:HIS893
|
2.4
|
15.0
|
1.0
|
SG
|
A:CYS896
|
2.4
|
15.0
|
1.0
|
SG
|
A:CYS873
|
2.6
|
15.0
|
1.0
|
SG
|
A:CYS870
|
2.7
|
15.0
|
1.0
|
HB3
|
A:CYS870
|
2.8
|
15.0
|
1.0
|
CB
|
A:HIS893
|
2.8
|
15.0
|
1.0
|
CG
|
A:HIS893
|
2.9
|
15.0
|
1.0
|
H
|
A:CYS873
|
3.0
|
15.0
|
1.0
|
CB
|
A:CYS870
|
3.1
|
15.0
|
1.0
|
H
|
A:HIS893
|
3.2
|
15.0
|
1.0
|
HB2
|
A:CYS870
|
3.3
|
15.0
|
1.0
|
HB2
|
A:CYS896
|
3.4
|
15.0
|
1.0
|
HB3
|
A:HIS893
|
3.5
|
15.0
|
1.0
|
CB
|
A:CYS896
|
3.5
|
15.0
|
1.0
|
CE1
|
A:HIS893
|
3.5
|
15.0
|
1.0
|
HB3
|
A:CYS873
|
3.5
|
15.0
|
1.0
|
CB
|
A:CYS873
|
3.7
|
15.0
|
1.0
|
HB3
|
A:CYS896
|
3.7
|
15.0
|
1.0
|
N
|
A:HIS893
|
3.9
|
15.0
|
1.0
|
N
|
A:CYS873
|
3.9
|
15.0
|
1.0
|
CA
|
A:HIS893
|
4.0
|
15.0
|
1.0
|
HE1
|
A:HIS893
|
4.0
|
15.0
|
1.0
|
HB2
|
A:LYS875
|
4.1
|
15.0
|
1.0
|
CD2
|
A:HIS893
|
4.2
|
15.0
|
1.0
|
HA3
|
A:GLY872
|
4.4
|
15.0
|
1.0
|
H
|
A:GLY872
|
4.4
|
15.0
|
1.0
|
H
|
A:LYS875
|
4.4
|
15.0
|
1.0
|
H
|
A:CYS896
|
4.4
|
15.0
|
1.0
|
CA
|
A:CYS873
|
4.4
|
15.0
|
1.0
|
NE2
|
A:HIS893
|
4.5
|
15.0
|
1.0
|
HB2
|
A:CYS873
|
4.6
|
15.0
|
1.0
|
CA
|
A:CYS870
|
4.6
|
15.0
|
1.0
|
H
|
A:ASN874
|
4.6
|
15.0
|
1.0
|
HA
|
A:HIS893
|
4.7
|
15.0
|
1.0
|
C
|
A:HIS893
|
4.8
|
15.0
|
1.0
|
CA
|
A:CYS896
|
4.9
|
15.0
|
1.0
|
HG2
|
A:PRO895
|
4.9
|
15.0
|
1.0
|
O
|
A:HIS893
|
4.9
|
15.0
|
1.0
|
C
|
A:GLY872
|
4.9
|
15.0
|
1.0
|
CA
|
A:GLY872
|
5.0
|
15.0
|
1.0
|
|
Reference:
L.Pulido-Cortes,
H.Gielingh,
V.Thijssen,
M.Liu,
R.Yoshisada,
L.R.Soares,
N.Sheikh,
F.Friedrich,
H.Greschik,
L.Peng,
R.V.Honorato,
M.Jung,
A.M.J.J.Bonvin,
M.L.Biniossek,
R.Schule,
H.Van Ingen,
H.T.M.Timmers,
S.Jongkees.
Molecular Determinants For Recognition of Serotonylated Chromatin To Be Published.
Page generated: Fri Aug 22 18:57:07 2025
|