Zinc in PDB 2kwj: Solution Structures of the Double Phd Fingers of Human Transcriptional Protein DPF3 Bound to A Histone Peptide Containing Acetylation at Lysine 14
Zinc Binding Sites:
The binding sites of Zinc atom in the Solution Structures of the Double Phd Fingers of Human Transcriptional Protein DPF3 Bound to A Histone Peptide Containing Acetylation at Lysine 14
(pdb code 2kwj). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the
Solution Structures of the Double Phd Fingers of Human Transcriptional Protein DPF3 Bound to A Histone Peptide Containing Acetylation at Lysine 14, PDB code: 2kwj:
Jump to Zinc binding site number:
1;
2;
3;
4;
Zinc binding site 1 out
of 4 in 2kwj
Go back to
Zinc Binding Sites List in 2kwj
Zinc binding site 1 out
of 4 in the Solution Structures of the Double Phd Fingers of Human Transcriptional Protein DPF3 Bound to A Histone Peptide Containing Acetylation at Lysine 14
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Solution Structures of the Double Phd Fingers of Human Transcriptional Protein DPF3 Bound to A Histone Peptide Containing Acetylation at Lysine 14 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn501
b:0.0
occ:1.00
|
ND1
|
A:HIS292
|
2.1
|
0.0
|
1.0
|
SG
|
A:CYS262
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS265
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS295
|
2.3
|
0.0
|
1.0
|
HB2
|
A:HIS292
|
2.7
|
0.0
|
1.0
|
HB3
|
A:CYS262
|
3.0
|
0.0
|
1.0
|
CE1
|
A:HIS292
|
3.1
|
0.0
|
1.0
|
CG
|
A:HIS292
|
3.1
|
0.0
|
1.0
|
H
|
A:CYS265
|
3.2
|
0.0
|
1.0
|
CB
|
A:CYS262
|
3.2
|
0.0
|
1.0
|
HE1
|
A:HIS292
|
3.3
|
0.0
|
1.0
|
HB3
|
A:CYS265
|
3.3
|
0.0
|
1.0
|
HB2
|
A:CYS295
|
3.3
|
0.0
|
1.0
|
HD21
|
A:ASN272
|
3.4
|
0.0
|
1.0
|
CB
|
A:CYS265
|
3.4
|
0.0
|
1.0
|
CB
|
A:CYS295
|
3.4
|
0.0
|
1.0
|
CB
|
A:HIS292
|
3.4
|
0.0
|
1.0
|
HB2
|
A:CYS262
|
3.5
|
0.0
|
1.0
|
H
|
A:HIS292
|
3.5
|
0.0
|
1.0
|
HB3
|
A:CYS295
|
3.6
|
0.0
|
1.0
|
HB2
|
A:PHE264
|
3.7
|
0.0
|
1.0
|
N
|
A:CYS265
|
3.7
|
0.0
|
1.0
|
H
|
A:GLY267
|
3.7
|
0.0
|
1.0
|
H
|
A:LEU266
|
3.8
|
0.0
|
1.0
|
ND2
|
A:ASN272
|
3.9
|
0.0
|
1.0
|
H
|
A:LYS273
|
4.0
|
0.0
|
1.0
|
CA
|
A:CYS265
|
4.0
|
0.0
|
1.0
|
HD22
|
A:ASN272
|
4.1
|
0.0
|
1.0
|
HB3
|
A:HIS292
|
4.1
|
0.0
|
1.0
|
H
|
A:PHE264
|
4.2
|
0.0
|
1.0
|
NE2
|
A:HIS292
|
4.2
|
0.0
|
1.0
|
CD2
|
A:HIS292
|
4.2
|
0.0
|
1.0
|
N
|
A:HIS292
|
4.3
|
0.0
|
1.0
|
HB2
|
A:CYS265
|
4.3
|
0.0
|
1.0
|
N
|
A:LEU266
|
4.3
|
0.0
|
1.0
|
HA
|
A:ASN272
|
4.4
|
0.0
|
1.0
|
CA
|
A:HIS292
|
4.5
|
0.0
|
1.0
|
C
|
A:CYS265
|
4.5
|
0.0
|
1.0
|
HG3
|
A:LYS274
|
4.6
|
0.0
|
1.0
|
CA
|
A:CYS262
|
4.6
|
0.0
|
1.0
|
C
|
A:PHE264
|
4.7
|
0.0
|
1.0
|
N
|
A:GLY267
|
4.7
|
0.0
|
1.0
|
H
|
A:CYS295
|
4.7
|
0.0
|
1.0
|
CB
|
A:PHE264
|
4.7
|
0.0
|
1.0
|
H
|
A:CYS262
|
4.8
|
0.0
|
1.0
|
HB3
|
A:ASN272
|
4.8
|
0.0
|
1.0
|
CA
|
A:CYS295
|
4.8
|
0.0
|
1.0
|
H
|
A:LYS274
|
4.8
|
0.0
|
1.0
|
CG
|
A:ASN272
|
4.9
|
0.0
|
1.0
|
N
|
A:PHE264
|
4.9
|
0.0
|
1.0
|
HD2
|
A:PHE264
|
4.9
|
0.0
|
1.0
|
HB2
|
A:LYS273
|
4.9
|
0.0
|
1.0
|
HA3
|
A:GLY267
|
4.9
|
0.0
|
1.0
|
HB2
|
A:LYS274
|
5.0
|
0.0
|
1.0
|
CA
|
A:PHE264
|
5.0
|
0.0
|
1.0
|
N
|
A:LYS273
|
5.0
|
0.0
|
1.0
|
|
Zinc binding site 2 out
of 4 in 2kwj
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Zinc Binding Sites List in 2kwj
Zinc binding site 2 out
of 4 in the Solution Structures of the Double Phd Fingers of Human Transcriptional Protein DPF3 Bound to A Histone Peptide Containing Acetylation at Lysine 14
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Solution Structures of the Double Phd Fingers of Human Transcriptional Protein DPF3 Bound to A Histone Peptide Containing Acetylation at Lysine 14 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn601
b:0.0
occ:1.00
|
SG
|
A:CYS284
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS316
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS313
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS287
|
2.3
|
0.0
|
1.0
|
H
|
A:CYS313
|
2.8
|
0.0
|
1.0
|
HB2
|
A:CYS316
|
3.1
|
0.0
|
1.0
|
H
|
A:CYS287
|
3.2
|
0.0
|
1.0
|
HB3
|
A:CYS287
|
3.3
|
0.0
|
1.0
|
HB3
|
A:CYS284
|
3.3
|
0.0
|
1.0
|
CB
|
A:CYS284
|
3.3
|
0.0
|
1.0
|
HB3
|
A:CYS313
|
3.3
|
0.0
|
1.0
|
CB
|
A:CYS316
|
3.3
|
0.0
|
1.0
|
CB
|
A:CYS313
|
3.4
|
0.0
|
1.0
|
CB
|
A:CYS287
|
3.4
|
0.0
|
1.0
|
HB3
|
A:ASP286
|
3.4
|
0.0
|
1.0
|
HB2
|
A:CYS284
|
3.4
|
0.0
|
1.0
|
N
|
A:CYS313
|
3.7
|
0.0
|
1.0
|
N
|
A:CYS287
|
3.8
|
0.0
|
1.0
|
HB3
|
A:CYS316
|
3.9
|
0.0
|
1.0
|
H
|
A:GLY288
|
4.0
|
0.0
|
1.0
|
CA
|
A:CYS313
|
4.1
|
0.0
|
1.0
|
H
|
A:CYS316
|
4.1
|
0.0
|
1.0
|
H
|
A:ARG289
|
4.1
|
0.0
|
1.0
|
O
|
A:CYS313
|
4.2
|
0.0
|
1.0
|
CA
|
A:CYS287
|
4.2
|
0.0
|
1.0
|
H
|
A:ASP286
|
4.3
|
0.0
|
1.0
|
HB2
|
A:CYS287
|
4.3
|
0.0
|
1.0
|
HB2
|
A:CYS313
|
4.3
|
0.0
|
1.0
|
HG3
|
A:ARG289
|
4.4
|
0.0
|
1.0
|
HA
|
A:GLN312
|
4.4
|
0.0
|
1.0
|
HB2
|
A:ARG289
|
4.4
|
0.0
|
1.0
|
CB
|
A:ASP286
|
4.5
|
0.0
|
1.0
|
C
|
A:CYS313
|
4.6
|
0.0
|
1.0
|
CA
|
A:CYS316
|
4.6
|
0.0
|
1.0
|
N
|
A:GLY288
|
4.7
|
0.0
|
1.0
|
N
|
A:CYS316
|
4.7
|
0.0
|
1.0
|
C
|
A:ASP286
|
4.7
|
0.0
|
1.0
|
CA
|
A:CYS284
|
4.7
|
0.0
|
1.0
|
OD1
|
A:ASP286
|
4.8
|
0.0
|
1.0
|
C
|
A:GLN312
|
4.8
|
0.0
|
1.0
|
HE3
|
B:ALY14
|
4.9
|
0.0
|
1.0
|
C
|
A:CYS287
|
4.9
|
0.0
|
1.0
|
N
|
A:ASP286
|
5.0
|
0.0
|
1.0
|
HZ
|
B:ALY14
|
5.0
|
0.0
|
1.0
|
CA
|
A:ASP286
|
5.0
|
0.0
|
1.0
|
HB3
|
A:GLN312
|
5.0
|
0.0
|
1.0
|
|
Zinc binding site 3 out
of 4 in 2kwj
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Zinc Binding Sites List in 2kwj
Zinc binding site 3 out
of 4 in the Solution Structures of the Double Phd Fingers of Human Transcriptional Protein DPF3 Bound to A Histone Peptide Containing Acetylation at Lysine 14
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Solution Structures of the Double Phd Fingers of Human Transcriptional Protein DPF3 Bound to A Histone Peptide Containing Acetylation at Lysine 14 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn701
b:0.0
occ:1.00
|
SG
|
A:CYS334
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS337
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS363
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS360
|
2.3
|
0.0
|
1.0
|
H
|
A:CYS337
|
2.4
|
0.0
|
1.0
|
H
|
A:ASP336
|
2.9
|
0.0
|
1.0
|
H
|
A:CYS363
|
3.0
|
0.0
|
1.0
|
HB3
|
A:LEU362
|
3.2
|
0.0
|
1.0
|
HB2
|
A:CYS334
|
3.2
|
0.0
|
1.0
|
N
|
A:CYS337
|
3.2
|
0.0
|
1.0
|
HB3
|
A:CYS360
|
3.3
|
0.0
|
1.0
|
HB3
|
A:ASP336
|
3.3
|
0.0
|
1.0
|
HB2
|
A:CYS337
|
3.4
|
0.0
|
1.0
|
HB2
|
A:ARG339
|
3.4
|
0.0
|
1.0
|
CB
|
A:CYS337
|
3.4
|
0.0
|
1.0
|
CB
|
A:CYS334
|
3.4
|
0.0
|
1.0
|
CB
|
A:CYS360
|
3.4
|
0.0
|
1.0
|
CB
|
A:CYS363
|
3.4
|
0.0
|
1.0
|
N
|
A:CYS363
|
3.5
|
0.0
|
1.0
|
H
|
A:ASP338
|
3.5
|
0.0
|
1.0
|
H
|
A:CYS360
|
3.5
|
0.0
|
1.0
|
HB2
|
A:CYS363
|
3.6
|
0.0
|
1.0
|
H
|
A:ASP335
|
3.6
|
0.0
|
1.0
|
HG3
|
A:ARG339
|
3.7
|
0.0
|
1.0
|
H
|
A:ARG339
|
3.8
|
0.0
|
1.0
|
N
|
A:ASP336
|
3.8
|
0.0
|
1.0
|
HA
|
A:CYS363
|
3.8
|
0.0
|
1.0
|
CA
|
A:CYS363
|
3.8
|
0.0
|
1.0
|
CA
|
A:CYS337
|
3.9
|
0.0
|
1.0
|
CB
|
A:ASP336
|
4.1
|
0.0
|
1.0
|
C
|
A:ASP336
|
4.1
|
0.0
|
1.0
|
N
|
A:CYS360
|
4.1
|
0.0
|
1.0
|
HB3
|
A:CYS334
|
4.1
|
0.0
|
1.0
|
HB2
|
A:ASP336
|
4.1
|
0.0
|
1.0
|
CA
|
A:ASP336
|
4.2
|
0.0
|
1.0
|
CB
|
A:LEU362
|
4.2
|
0.0
|
1.0
|
CA
|
A:CYS360
|
4.3
|
0.0
|
1.0
|
HD11
|
A:LEU362
|
4.3
|
0.0
|
1.0
|
HB2
|
A:CYS360
|
4.3
|
0.0
|
1.0
|
N
|
A:ASP335
|
4.3
|
0.0
|
1.0
|
HB3
|
A:CYS337
|
4.3
|
0.0
|
1.0
|
CB
|
A:ARG339
|
4.4
|
0.0
|
1.0
|
HB3
|
A:CYS363
|
4.4
|
0.0
|
1.0
|
N
|
A:ASP338
|
4.4
|
0.0
|
1.0
|
C
|
A:LEU362
|
4.4
|
0.0
|
1.0
|
HA
|
A:CYS334
|
4.4
|
0.0
|
1.0
|
CA
|
A:CYS334
|
4.4
|
0.0
|
1.0
|
CG
|
A:ARG339
|
4.5
|
0.0
|
1.0
|
H
|
A:LEU362
|
4.5
|
0.0
|
1.0
|
C
|
A:CYS360
|
4.6
|
0.0
|
1.0
|
HH
|
A:TYR341
|
4.6
|
0.0
|
1.0
|
HB2
|
A:LEU362
|
4.6
|
0.0
|
1.0
|
N
|
A:ARG339
|
4.7
|
0.0
|
1.0
|
CA
|
A:LEU362
|
4.7
|
0.0
|
1.0
|
C
|
A:CYS337
|
4.7
|
0.0
|
1.0
|
N
|
A:LEU362
|
4.8
|
0.0
|
1.0
|
O
|
A:CYS360
|
4.8
|
0.0
|
1.0
|
C
|
A:CYS334
|
4.8
|
0.0
|
1.0
|
HA
|
A:CYS337
|
4.8
|
0.0
|
1.0
|
HG2
|
A:ARG339
|
4.8
|
0.0
|
1.0
|
HE3
|
A:MET302
|
4.9
|
0.0
|
1.0
|
C
|
A:ASP335
|
4.9
|
0.0
|
1.0
|
HA
|
A:SER359
|
5.0
|
0.0
|
1.0
|
|
Zinc binding site 4 out
of 4 in 2kwj
Go back to
Zinc Binding Sites List in 2kwj
Zinc binding site 4 out
of 4 in the Solution Structures of the Double Phd Fingers of Human Transcriptional Protein DPF3 Bound to A Histone Peptide Containing Acetylation at Lysine 14
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Solution Structures of the Double Phd Fingers of Human Transcriptional Protein DPF3 Bound to A Histone Peptide Containing Acetylation at Lysine 14 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn801
b:0.0
occ:1.00
|
ND1
|
A:HIS342
|
2.1
|
0.0
|
1.0
|
SG
|
A:CYS319
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS322
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS345
|
2.3
|
0.0
|
1.0
|
HB2
|
A:HIS342
|
2.7
|
0.0
|
1.0
|
HB3
|
A:CYS319
|
3.0
|
0.0
|
1.0
|
CE1
|
A:HIS342
|
3.0
|
0.0
|
1.0
|
CG
|
A:HIS342
|
3.1
|
0.0
|
1.0
|
CB
|
A:CYS319
|
3.2
|
0.0
|
1.0
|
HB3
|
A:CYS322
|
3.3
|
0.0
|
1.0
|
HE1
|
A:HIS342
|
3.3
|
0.0
|
1.0
|
H
|
A:CYS322
|
3.3
|
0.0
|
1.0
|
H
|
A:HIS342
|
3.4
|
0.0
|
1.0
|
CB
|
A:HIS342
|
3.4
|
0.0
|
1.0
|
CB
|
A:CYS322
|
3.4
|
0.0
|
1.0
|
CB
|
A:CYS345
|
3.4
|
0.0
|
1.0
|
HB2
|
A:CYS345
|
3.4
|
0.0
|
1.0
|
HB2
|
A:LEU321
|
3.5
|
0.0
|
1.0
|
HB3
|
A:CYS345
|
3.5
|
0.0
|
1.0
|
HB2
|
A:CYS319
|
3.6
|
0.0
|
1.0
|
N
|
A:CYS322
|
3.9
|
0.0
|
1.0
|
HG1
|
A:THR324
|
4.0
|
0.0
|
1.0
|
HB3
|
A:HIS342
|
4.1
|
0.0
|
1.0
|
OG1
|
A:THR324
|
4.1
|
0.0
|
1.0
|
CA
|
A:CYS322
|
4.2
|
0.0
|
1.0
|
NE2
|
A:HIS342
|
4.2
|
0.0
|
1.0
|
N
|
A:HIS342
|
4.2
|
0.0
|
1.0
|
H
|
A:SER325
|
4.2
|
0.0
|
1.0
|
CD2
|
A:HIS342
|
4.2
|
0.0
|
1.0
|
H
|
A:THR324
|
4.2
|
0.0
|
1.0
|
HB2
|
A:CYS322
|
4.3
|
0.0
|
1.0
|
O
|
A:CYS319
|
4.3
|
0.0
|
1.0
|
CA
|
A:HIS342
|
4.4
|
0.0
|
1.0
|
CA
|
A:CYS319
|
4.6
|
0.0
|
1.0
|
CB
|
A:LEU321
|
4.6
|
0.0
|
1.0
|
HG21
|
A:THR324
|
4.7
|
0.0
|
1.0
|
C
|
A:CYS322
|
4.7
|
0.0
|
1.0
|
H
|
A:GLY323
|
4.8
|
0.0
|
1.0
|
C
|
A:CYS319
|
4.8
|
0.0
|
1.0
|
CA
|
A:CYS345
|
4.8
|
0.0
|
1.0
|
C
|
A:LEU321
|
4.8
|
0.0
|
1.0
|
OE1
|
A:GLU326
|
4.9
|
0.0
|
1.0
|
H
|
A:GLU326
|
5.0
|
0.0
|
1.0
|
HA
|
A:TYR341
|
5.0
|
0.0
|
1.0
|
N
|
A:GLY323
|
5.0
|
0.0
|
1.0
|
|
Reference:
L.Zeng,
Q.Zhang,
S.Li,
A.N.Plotnikov,
M.J.Walsh,
M.M.Zhou.
Mechanism and Regulation of Acetylated Histone Binding By the Tandem Phd Finger of DPF3B. Nature V. 466 258 2010.
ISSN: ISSN 0028-0836
PubMed: 20613843
DOI: 10.1038/NATURE09139
Page generated: Thu Oct 17 01:40:33 2024
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