Zinc in PDB 8f8z: PHF2 (Phd+Jmj) in Complex with H3 Histone N-Terminal Peptide
Protein crystallography data
The structure of PHF2 (Phd+Jmj) in Complex with H3 Histone N-Terminal Peptide, PDB code: 8f8z
was solved by
J.R.Horton,
X.Cheng,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
54.50 /
3.30
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
73.854,
83.756,
104.128,
90,
103.67,
90
|
R / Rfree (%)
|
21.3 /
25.6
|
Zinc Binding Sites:
The binding sites of Zinc atom in the PHF2 (Phd+Jmj) in Complex with H3 Histone N-Terminal Peptide
(pdb code 8f8z). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the
PHF2 (Phd+Jmj) in Complex with H3 Histone N-Terminal Peptide, PDB code: 8f8z:
Jump to Zinc binding site number:
1;
2;
3;
4;
Zinc binding site 1 out
of 4 in 8f8z
Go back to
Zinc Binding Sites List in 8f8z
Zinc binding site 1 out
of 4 in the PHF2 (Phd+Jmj) in Complex with H3 Histone N-Terminal Peptide
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of PHF2 (Phd+Jmj) in Complex with H3 Histone N-Terminal Peptide within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn501
b:58.0
occ:1.00
|
SG
|
A:CYS50
|
2.2
|
59.6
|
1.0
|
SG
|
A:CYS23
|
2.3
|
59.8
|
1.0
|
SG
|
A:CYS26
|
2.3
|
53.3
|
1.0
|
SG
|
A:CYS53
|
2.4
|
59.4
|
1.0
|
CB
|
A:CYS23
|
3.1
|
50.6
|
1.0
|
CB
|
A:CYS50
|
3.3
|
57.7
|
1.0
|
CB
|
A:CYS53
|
3.3
|
59.1
|
1.0
|
CB
|
A:CYS26
|
3.5
|
56.1
|
1.0
|
N
|
A:CYS50
|
3.7
|
58.3
|
1.0
|
N
|
A:CYS26
|
3.8
|
59.4
|
1.0
|
CE1
|
A:PHE30
|
4.0
|
56.6
|
1.0
|
CA
|
A:CYS50
|
4.1
|
60.9
|
1.0
|
CZ
|
A:PHE30
|
4.1
|
56.6
|
1.0
|
CA
|
A:CYS26
|
4.3
|
57.7
|
1.0
|
N
|
A:CYS53
|
4.4
|
62.1
|
1.0
|
CA
|
A:CYS53
|
4.5
|
59.0
|
1.0
|
CB
|
A:ALA25
|
4.5
|
57.4
|
1.0
|
CA
|
A:CYS23
|
4.5
|
52.5
|
1.0
|
O
|
A:CYS50
|
4.7
|
77.2
|
1.0
|
C
|
A:CYS50
|
4.7
|
72.5
|
1.0
|
C
|
A:ALA25
|
4.9
|
59.2
|
1.0
|
C
|
A:HIS49
|
4.9
|
58.2
|
1.0
|
C
|
A:CYS23
|
4.9
|
57.0
|
1.0
|
N
|
A:ALA25
|
4.9
|
61.0
|
1.0
|
|
Zinc binding site 2 out
of 4 in 8f8z
Go back to
Zinc Binding Sites List in 8f8z
Zinc binding site 2 out
of 4 in the PHF2 (Phd+Jmj) in Complex with H3 Histone N-Terminal Peptide
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of PHF2 (Phd+Jmj) in Complex with H3 Histone N-Terminal Peptide within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn502
b:76.5
occ:1.00
|
ND1
|
A:HIS31
|
2.1
|
70.9
|
1.0
|
SG
|
A:CYS34
|
2.1
|
51.8
|
1.0
|
SG
|
A:CYS8
|
2.3
|
60.2
|
1.0
|
SG
|
A:CYS10
|
2.3
|
60.9
|
1.0
|
CG
|
A:HIS31
|
2.7
|
64.7
|
1.0
|
CB
|
A:HIS31
|
2.9
|
62.4
|
1.0
|
CB
|
A:CYS8
|
3.1
|
65.3
|
1.0
|
CE1
|
A:HIS31
|
3.1
|
64.5
|
1.0
|
CB
|
A:CYS34
|
3.4
|
61.7
|
1.0
|
N
|
A:HIS31
|
3.7
|
57.7
|
1.0
|
CB
|
A:CYS10
|
3.8
|
68.9
|
1.0
|
CD2
|
A:HIS31
|
3.9
|
66.4
|
1.0
|
CA
|
A:HIS31
|
3.9
|
60.2
|
1.0
|
NE2
|
A:HIS31
|
4.1
|
63.2
|
1.0
|
NH2
|
A:ARG18
|
4.3
|
66.8
|
1.0
|
N
|
A:CYS10
|
4.5
|
79.5
|
1.0
|
NH1
|
A:ARG18
|
4.5
|
66.6
|
1.0
|
CA
|
A:CYS8
|
4.6
|
62.1
|
1.0
|
CZ
|
A:ARG18
|
4.6
|
65.9
|
1.0
|
CA
|
A:CYS34
|
4.6
|
67.2
|
1.0
|
N
|
A:CYS34
|
4.7
|
65.3
|
1.0
|
CA
|
A:CYS10
|
4.8
|
73.5
|
1.0
|
N
|
A:VAL9
|
4.9
|
72.5
|
1.0
|
C
|
A:HIS31
|
4.9
|
62.6
|
1.0
|
C
|
A:PHE30
|
5.0
|
54.4
|
1.0
|
|
Zinc binding site 3 out
of 4 in 8f8z
Go back to
Zinc Binding Sites List in 8f8z
Zinc binding site 3 out
of 4 in the PHF2 (Phd+Jmj) in Complex with H3 Histone N-Terminal Peptide
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of PHF2 (Phd+Jmj) in Complex with H3 Histone N-Terminal Peptide within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn501
b:61.6
occ:1.00
|
SG
|
B:CYS53
|
2.2
|
66.0
|
1.0
|
SG
|
B:CYS26
|
2.2
|
53.5
|
1.0
|
SG
|
B:CYS50
|
2.3
|
65.3
|
1.0
|
SG
|
B:CYS23
|
2.4
|
60.3
|
1.0
|
CB
|
B:CYS23
|
3.1
|
58.7
|
1.0
|
CB
|
B:CYS53
|
3.3
|
66.3
|
1.0
|
CB
|
B:CYS50
|
3.4
|
62.3
|
1.0
|
CB
|
B:CYS26
|
3.4
|
53.6
|
1.0
|
N
|
B:CYS26
|
3.8
|
61.0
|
1.0
|
N
|
B:CYS50
|
3.9
|
66.0
|
1.0
|
CE1
|
B:PHE30
|
4.0
|
54.5
|
1.0
|
CZ
|
B:PHE30
|
4.1
|
56.9
|
1.0
|
CA
|
B:CYS50
|
4.2
|
66.7
|
1.0
|
CA
|
B:CYS26
|
4.2
|
57.2
|
1.0
|
N
|
B:CYS53
|
4.3
|
72.7
|
1.0
|
CA
|
B:CYS53
|
4.4
|
70.5
|
1.0
|
CB
|
B:ALA25
|
4.5
|
67.1
|
1.0
|
CA
|
B:CYS23
|
4.6
|
55.8
|
1.0
|
O
|
B:CYS50
|
4.8
|
71.3
|
1.0
|
C
|
B:CYS50
|
4.8
|
69.2
|
1.0
|
C
|
B:ALA25
|
4.8
|
61.5
|
1.0
|
C
|
B:CYS23
|
4.9
|
59.1
|
1.0
|
C
|
B:CYS26
|
5.0
|
55.9
|
1.0
|
N
|
B:ALA25
|
5.0
|
60.6
|
1.0
|
|
Zinc binding site 4 out
of 4 in 8f8z
Go back to
Zinc Binding Sites List in 8f8z
Zinc binding site 4 out
of 4 in the PHF2 (Phd+Jmj) in Complex with H3 Histone N-Terminal Peptide
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of PHF2 (Phd+Jmj) in Complex with H3 Histone N-Terminal Peptide within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn502
b:66.2
occ:1.00
|
ND1
|
B:HIS31
|
2.1
|
67.5
|
1.0
|
SG
|
B:CYS34
|
2.2
|
65.6
|
1.0
|
SG
|
B:CYS10
|
2.4
|
66.8
|
1.0
|
SG
|
B:CYS8
|
2.4
|
57.8
|
1.0
|
CG
|
B:HIS31
|
2.9
|
64.2
|
1.0
|
CB
|
B:HIS31
|
3.0
|
62.9
|
1.0
|
CE1
|
B:HIS31
|
3.1
|
71.2
|
1.0
|
CB
|
B:CYS34
|
3.2
|
61.4
|
1.0
|
CB
|
B:CYS8
|
3.3
|
60.8
|
1.0
|
CB
|
B:CYS10
|
3.7
|
65.8
|
1.0
|
N
|
B:HIS31
|
3.8
|
57.5
|
1.0
|
CA
|
B:HIS31
|
4.0
|
61.0
|
1.0
|
CD2
|
B:HIS31
|
4.0
|
64.7
|
1.0
|
NE2
|
B:HIS31
|
4.1
|
66.5
|
1.0
|
N
|
B:CYS10
|
4.2
|
76.9
|
1.0
|
NH2
|
B:ARG18
|
4.3
|
68.2
|
1.0
|
NH1
|
B:ARG18
|
4.5
|
70.2
|
1.0
|
CA
|
B:CYS10
|
4.6
|
68.2
|
1.0
|
CA
|
B:CYS34
|
4.6
|
64.2
|
1.0
|
CZ
|
B:ARG18
|
4.6
|
70.7
|
1.0
|
N
|
B:VAL9
|
4.7
|
75.6
|
1.0
|
CA
|
B:CYS8
|
4.7
|
63.3
|
1.0
|
CG2
|
B:VAL9
|
4.8
|
81.5
|
1.0
|
N
|
B:CYS34
|
4.9
|
68.0
|
1.0
|
O
|
B:HIS31
|
4.9
|
62.7
|
1.0
|
C
|
B:HIS31
|
4.9
|
62.4
|
1.0
|
|
Reference:
J.R.Horton,
J.Zhou,
Q.Chen,
X.Zhang,
M.T.Bedford,
X.Cheng.
A Complete Methyl-Lysine Binding Aromatic Cage Constructed By Two Domains of PHF2. J.Biol.Chem. 02862 2022.
ISSN: ESSN 1083-351X
PubMed: 36596360
DOI: 10.1016/J.JBC.2022.102862
Page generated: Wed Oct 30 20:15:28 2024
|