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Zinc in PDB 4n4f: Crystal Structure of the Bromodomain-Phd Finger Module of Human Transcriptional Co-Activator Cbp in Complex with Di-Acetylated Histone 4 Peptide (H412ACK16AC).

Enzymatic activity of Crystal Structure of the Bromodomain-Phd Finger Module of Human Transcriptional Co-Activator Cbp in Complex with Di-Acetylated Histone 4 Peptide (H412ACK16AC).

All present enzymatic activity of Crystal Structure of the Bromodomain-Phd Finger Module of Human Transcriptional Co-Activator Cbp in Complex with Di-Acetylated Histone 4 Peptide (H412ACK16AC).:
2.3.1.48;

Protein crystallography data

The structure of Crystal Structure of the Bromodomain-Phd Finger Module of Human Transcriptional Co-Activator Cbp in Complex with Di-Acetylated Histone 4 Peptide (H412ACK16AC)., PDB code: 4n4f was solved by A.N.Plotnikov, J.Zhou, M.-M.Zhou, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.69 / 1.83
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 92.010, 59.460, 53.880, 90.00, 102.68, 90.00
R / Rfree (%) 21 / 24.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Bromodomain-Phd Finger Module of Human Transcriptional Co-Activator Cbp in Complex with Di-Acetylated Histone 4 Peptide (H412ACK16AC). (pdb code 4n4f). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the Bromodomain-Phd Finger Module of Human Transcriptional Co-Activator Cbp in Complex with Di-Acetylated Histone 4 Peptide (H412ACK16AC)., PDB code: 4n4f:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 4n4f

Go back to Zinc Binding Sites List in 4n4f
Zinc binding site 1 out of 2 in the Crystal Structure of the Bromodomain-Phd Finger Module of Human Transcriptional Co-Activator Cbp in Complex with Di-Acetylated Histone 4 Peptide (H412ACK16AC).


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Bromodomain-Phd Finger Module of Human Transcriptional Co-Activator Cbp in Complex with Di-Acetylated Histone 4 Peptide (H412ACK16AC). within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1401

b:34.8
occ:1.00
ND1 A:HIS1291 2.1 30.6 1.0
SG A:CYS1199 2.3 34.7 1.0
SG A:CYS1294 2.3 33.4 1.0
SG A:CYS1200 2.4 33.1 1.0
CE1 A:HIS1291 3.1 32.7 1.0
CG A:HIS1291 3.1 34.7 1.0
CB A:CYS1199 3.3 35.0 1.0
CB A:CYS1294 3.3 33.1 1.0
CB A:HIS1291 3.4 33.2 1.0
CB A:CYS1200 3.5 32.0 1.0
N A:CYS1200 3.6 34.0 1.0
C A:CYS1199 3.9 33.2 1.0
CA A:CYS1200 4.0 34.4 1.0
NE2 A:HIS1291 4.2 35.5 1.0
CA A:CYS1199 4.2 33.1 1.0
CD2 A:HIS1291 4.2 34.8 1.0
N A:HIS1291 4.2 32.9 1.0
O A:HOH1524 4.3 39.1 1.0
CA A:HIS1291 4.4 32.7 1.0
C A:CYS1200 4.5 34.8 1.0
O A:CYS1200 4.6 31.0 1.0
O A:CYS1199 4.6 33.2 1.0
CA A:CYS1294 4.7 31.2 1.0
O A:HOH1549 4.7 48.7 1.0
NH2 A:ARG1202 4.8 44.7 1.0
N A:CYS1199 4.9 34.4 1.0

Zinc binding site 2 out of 2 in 4n4f

Go back to Zinc Binding Sites List in 4n4f
Zinc binding site 2 out of 2 in the Crystal Structure of the Bromodomain-Phd Finger Module of Human Transcriptional Co-Activator Cbp in Complex with Di-Acetylated Histone 4 Peptide (H412ACK16AC).


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the Bromodomain-Phd Finger Module of Human Transcriptional Co-Activator Cbp in Complex with Di-Acetylated Histone 4 Peptide (H412ACK16AC). within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1402

b:43.9
occ:1.00
SG A:CYS1308 2.3 45.4 1.0
SG A:CYS1311 2.3 46.4 1.0
SG A:CYS1283 2.3 41.5 1.0
SG A:CYS1286 2.4 40.6 1.0
CB A:CYS1283 3.2 38.9 1.0
CB A:CYS1311 3.2 53.0 1.0
CB A:CYS1286 3.3 39.0 1.0
CB A:CYS1308 3.4 48.2 1.0
N A:CYS1286 3.6 41.8 1.0
N A:CYS1308 4.0 47.9 1.0
CA A:CYS1286 4.1 38.9 1.0
CA A:CYS1308 4.2 48.4 1.0
N A:CYS1311 4.3 53.2 1.0
CA A:CYS1311 4.4 53.2 1.0
CB A:GLU1285 4.5 46.3 1.0
CA A:CYS1283 4.7 38.2 1.0
O A:CYS1308 4.7 49.4 1.0
C A:GLU1285 4.7 47.8 1.0
C A:CYS1308 4.8 52.6 1.0
NH1 A:ARG1288 4.8 42.0 1.0
C A:CYS1286 4.9 38.2 1.0
ND2 A:ASN1310 4.9 61.7 1.0
CB A:ASN1310 4.9 66.5 1.0
N A:GLY1287 5.0 41.8 1.0

Reference:

A.N.Plotnikov, S.Yang, T.J.Zhou, E.Rusinova, A.Frasca, M.M.Zhou. Structural Insights Into Acetylated-Histone H4 Recognition By the Bromodomain-Phd Finger Module of Human Transcriptional Coactivator Cbp. Structure V. 22 353 2014.
ISSN: ISSN 0969-2126
PubMed: 24361270
DOI: 10.1016/J.STR.2013.10.021
Page generated: Sun Oct 27 02:59:50 2024

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