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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

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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 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 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

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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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