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Zinc in PDB 8cnd: Crystal Structure of Crebbp-Y1482N Histone Acetyltransferase Domain in Complex with A Bisubstrate Inhibitor, Lys-Coa

Enzymatic activity of Crystal Structure of Crebbp-Y1482N Histone Acetyltransferase Domain in Complex with A Bisubstrate Inhibitor, Lys-Coa

All present enzymatic activity of Crystal Structure of Crebbp-Y1482N Histone Acetyltransferase Domain in Complex with A Bisubstrate Inhibitor, Lys-Coa:
2.3.1.48;

Protein crystallography data

The structure of Crystal Structure of Crebbp-Y1482N Histone Acetyltransferase Domain in Complex with A Bisubstrate Inhibitor, Lys-Coa, PDB code: 8cnd was solved by A.E.Mechaly, W.Zhang, A.Haouz, M.Green, F.Rodrigues-Lima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 77.46 / 2.97
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 86.81, 149.195, 154.918, 90, 90, 90
R / Rfree (%) 27.8 / 32.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Crebbp-Y1482N Histone Acetyltransferase Domain in Complex with A Bisubstrate Inhibitor, Lys-Coa (pdb code 8cnd). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 5 binding sites of Zinc where determined in the Crystal Structure of Crebbp-Y1482N Histone Acetyltransferase Domain in Complex with A Bisubstrate Inhibitor, Lys-Coa, PDB code: 8cnd:
Jump to Zinc binding site number: 1; 2; 3; 4; 5;

Zinc binding site 1 out of 5 in 8cnd

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Zinc binding site 1 out of 5 in the Crystal Structure of Crebbp-Y1482N Histone Acetyltransferase Domain in Complex with A Bisubstrate Inhibitor, Lys-Coa


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 Crebbp-Y1482N Histone Acetyltransferase Domain in Complex with A Bisubstrate Inhibitor, Lys-Coa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1801

b:77.7
occ:1.00
 ND1 A:HIS1291 1.9 73.7 1.0
SG A:CYS1294 2.3 78.4 1.0
SG A:CYS1200 2.3 78.7 1.0
SG A:CYS1199 2.5 77.7 1.0
CG A:HIS1291 2.9 72.4 1.0
CE1 A:HIS1291 2.9 74.0 1.0
CB A:CYS1294 3.2 72.7 1.0
CB A:HIS1291 3.3 71.5 1.0
CB A:CYS1199 3.3 75.5 1.0
CB A:CYS1200 3.6 75.0 1.0
N A:CYS1200 3.7 74.6 1.0
N A:HIS1291 4.1 71.7 1.0
NE2 A:HIS1291 4.1 74.2 1.0
CD2 A:HIS1291 4.1 73.2 1.0
C A:CYS1199 4.1 75.4 1.0
CA A:CYS1200 4.2 74.0 1.0
CA A:HIS1291 4.3 71.5 1.0
CA A:CYS1199 4.3 75.7 1.0
NH2 A:ARG1681 4.6 64.0 1.0
CE2 A:TYR1204 4.6 69.8 1.0
CA A:CYS1294 4.6 71.4 1.0
O A:CYS1200 4.6 72.8 1.0
C A:CYS1200 4.7 72.8 1.0
O A:CYS1199 4.8 75.4 1.0
O A:HIS1291 4.9 71.6 1.0
CH2 A:TRP1151 4.9 78.5 1.0
CD2 A:TYR1204 5.0 69.1 1.0

Zinc binding site 2 out of 5 in 8cnd

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Zinc binding site 2 out of 5 in the Crystal Structure of Crebbp-Y1482N Histone Acetyltransferase Domain in Complex with A Bisubstrate Inhibitor, Lys-Coa


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 Crebbp-Y1482N Histone Acetyltransferase Domain in Complex with A Bisubstrate Inhibitor, Lys-Coa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1802

b:91.7
occ:1.00
 SG A:CYS1308 2.2 97.1 1.0
SG A:CYS1283 2.4 87.1 1.0
SG A:CYS1311 2.4 112.4 1.0
SG A:CYS1286 2.6 82.8 1.0
CB A:CYS1286 3.0 81.0 1.0
N A:CYS1286 3.3 81.7 1.0
CB A:CYS1308 3.4 94.4 1.0
CB A:CYS1311 3.5 108.4 1.0
CB A:CYS1283 3.6 84.3 1.0
CA A:CYS1286 3.8 80.7 1.0
N A:CYS1308 4.0 92.2 1.0
OD1 A:ASN1310 4.1 114.7 1.0
CA A:CYS1308 4.2 94.1 1.0
C A:GLU1285 4.4 83.2 1.0
NH1 A:ARG1288 4.5 92.0 1.0
CB A:GLU1285 4.5 87.7 1.0
CA A:CYS1311 4.6 108.1 1.0
N A:CYS1311 4.6 107.1 1.0
C A:CYS1286 4.8 79.5 1.0
CA A:GLU1285 4.8 84.2 1.0
N A:GLU1285 4.9 84.3 1.0
C A:CYS1308 4.9 96.6 1.0
O A:CYS1308 4.9 96.6 1.0
N A:GLY1287 5.0 78.3 1.0
CA A:CYS1283 5.0 84.0 1.0

Zinc binding site 3 out of 5 in 8cnd

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Zinc binding site 3 out of 5 in the Crystal Structure of Crebbp-Y1482N Histone Acetyltransferase Domain in Complex with A Bisubstrate Inhibitor, Lys-Coa


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Crebbp-Y1482N Histone Acetyltransferase Domain in Complex with A Bisubstrate Inhibitor, Lys-Coa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1803

b:169.4
occ:1.00
 CB A:CYS1709 1.9 145.8 1.0
O A:CYS1728 2.6 157.8 1.0
SG A:CYS1709 2.6 148.1 1.0
CA A:CYS1709 3.0 145.4 1.0
N A:CYS1709 3.0 145.3 1.0
CB A:CYS1728 3.0 158.4 1.0
N A:CYS1728 3.0 157.5 1.0
CA A:CYS1728 3.3 157.7 1.0
C A:CYS1728 3.3 157.7 1.0
CB A:CYS1706 3.7 143.9 1.0
SG A:CYS1706 3.8 148.1 1.0
C A:GLU1708 4.1 145.5 1.0
C A:CYS1709 4.2 145.4 1.0
C A:LEU1727 4.3 157.6 1.0
SG A:CYS1728 4.4 161.3 1.0
CD1 A:LEU1727 4.4 159.3 1.0
CG A:LEU1727 4.5 159.0 1.0
N A:LYS1710 4.6 145.2 1.0
N A:ILE1729 4.6 157.3 1.0
O A:ASN1730 4.6 157.8 1.0
CA A:LEU1727 4.7 157.3 1.0
N A:GLU1708 4.7 144.8 1.0
CA A:GLU1708 4.8 145.2 1.0
ND1 A:HIS1711 4.9 150.4 1.0
CB A:GLU1708 4.9 146.9 1.0
O A:GLU1708 4.9 145.8 1.0

Zinc binding site 4 out of 5 in 8cnd

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Zinc binding site 4 out of 5 in the Crystal Structure of Crebbp-Y1482N Histone Acetyltransferase Domain in Complex with A Bisubstrate Inhibitor, Lys-Coa


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Crebbp-Y1482N Histone Acetyltransferase Domain in Complex with A Bisubstrate Inhibitor, Lys-Coa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1804

b:174.0
occ:1.00
 SG A:CYS1722 2.3 154.7 1.0
SG A:CYS1719 2.4 154.5 1.0
ND1 A:HIS1740 2.5 160.8 1.0
CG A:HIS1740 2.6 158.8 1.0
NE2 A:HIS1738 2.7 159.2 1.0
CB A:HIS1740 2.8 156.4 1.0
CE1 A:HIS1740 3.2 161.3 1.0
CD2 A:HIS1740 3.3 160.1 1.0
CE1 A:HIS1738 3.6 159.6 1.0
NE2 A:HIS1740 3.7 161.2 1.0
CB A:CYS1719 3.7 149.8 1.0
CD2 A:HIS1738 3.7 158.2 1.0
CB A:CYS1722 3.8 151.6 1.0
N A:CYS1722 3.8 150.3 1.0
CB A:VAL1721 4.2 150.9 1.0
CA A:HIS1740 4.3 155.3 1.0
CG A:TYR1725 4.4 156.4 1.0
CA A:CYS1722 4.4 151.0 1.0
CB A:TYR1725 4.5 155.4 1.0
CD2 A:TYR1725 4.6 157.4 1.0
CG1 A:VAL1721 4.6 151.6 1.0
N A:HIS1740 4.7 154.9 1.0
CD1 A:TYR1725 4.7 157.4 1.0
C A:VAL1721 4.7 150.3 1.0
ND1 A:HIS1738 4.8 159.0 1.0
CA A:VAL1721 4.8 150.2 1.0
CG A:HIS1738 4.8 157.3 1.0
N A:VAL1721 4.9 149.8 1.0

Zinc binding site 5 out of 5 in 8cnd

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Zinc binding site 5 out of 5 in the Crystal Structure of Crebbp-Y1482N Histone Acetyltransferase Domain in Complex with A Bisubstrate Inhibitor, Lys-Coa


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Crystal Structure of Crebbp-Y1482N Histone Acetyltransferase Domain in Complex with A Bisubstrate Inhibitor, Lys-Coa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1806

b:113.1
occ:0.50
 CB A:CYS1444 2.5 94.9 1.0
CE1 A:HIS1351 2.7 115.5 1.0
SG A:CYS1444 3.0 100.1 1.0
NE2 A:HIS1351 3.4 115.5 1.0
ND1 A:HIS1351 3.6 115.1 1.0
CA A:CYS1444 4.0 93.8 1.0
CD2 A:LEU1445 4.3 95.1 1.0
CG A:LEU1445 4.4 94.3 1.0
C A:CYS1444 4.4 93.3 1.0
N A:LEU1445 4.4 92.1 1.0
CD2 A:HIS1351 4.4 114.5 1.0
CG A:HIS1351 4.5 113.5 1.0
N A:CYS1444 4.8 93.5 1.0

Reference:

A.E.Mechaly, W.Zhang, A.Haouz, M.Green, F.Rodrigues-Lima. Crystal Structure of Crebbp-Y1482N Histone Acetyltransferase Domain in Complex with A Bisubstrate Inhibitor, Lys-Coa To Be Published.
Page generated: Fri Aug 22 08:59:30 2025

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