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

Go back to Zinc Binding Sites List in 8cnd
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

Go back to Zinc Binding Sites List in 8cnd
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

Go back to Zinc Binding Sites List in 8cnd
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

Go back to Zinc Binding Sites List in 8cnd
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

Go back to Zinc Binding Sites List in 8cnd
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: Wed Oct 30 18:49:51 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy