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Zinc in PDB 4bhw: Structural Basis For Autoinhibition of the Acetyltransferase Activity of P300

Enzymatic activity of Structural Basis For Autoinhibition of the Acetyltransferase Activity of P300

All present enzymatic activity of Structural Basis For Autoinhibition of the Acetyltransferase Activity of P300:
2.3.1.48;

Protein crystallography data

The structure of Structural Basis For Autoinhibition of the Acetyltransferase Activity of P300, PDB code: 4bhw was solved by M.Delvecchio, J.Gaucher, C.Aguilar-Gurrieri, E.Ortega, D.Panne, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.620 / 2.80
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 153.051, 92.894, 123.309, 90.00, 98.43, 90.00
R / Rfree (%) 20.77 / 24.41

Zinc Binding Sites:

The binding sites of Zinc atom in the Structural Basis For Autoinhibition of the Acetyltransferase Activity of P300 (pdb code 4bhw). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 7 binding sites of Zinc where determined in the Structural Basis For Autoinhibition of the Acetyltransferase Activity of P300, PDB code: 4bhw:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7;

Zinc binding site 1 out of 7 in 4bhw

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Zinc binding site 1 out of 7 in the Structural Basis For Autoinhibition of the Acetyltransferase Activity of P300


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structural Basis For Autoinhibition of the Acetyltransferase Activity of P300 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1

b:59.3
occ:1.00
 SG A:CYS1163 2.2 62.0 1.0
ND1 A:HIS1255 2.3 61.5 1.0
SG A:CYS1164 2.3 57.6 1.0
SG A:CYS1258 2.4 69.2 1.0
CG A:HIS1255 3.1 61.5 1.0
CB A:HIS1255 3.3 57.4 1.0
CE1 A:HIS1255 3.3 65.2 1.0
CB A:CYS1164 3.3 61.5 1.0
CB A:CYS1258 3.4 60.5 1.0
CB A:CYS1163 3.4 59.5 1.0
N A:CYS1164 3.4 65.3 1.0
C A:CYS1163 3.9 65.0 1.0
CA A:CYS1164 3.9 66.2 1.0
CA A:CYS1163 4.2 61.4 1.0
CD2 A:HIS1255 4.3 67.3 1.0
N A:HIS1255 4.3 57.4 1.0
NE2 A:HIS1255 4.4 66.6 1.0
CA A:HIS1255 4.4 57.9 1.0
O A:CYS1163 4.5 68.3 1.0
C A:CYS1164 4.5 69.5 1.0
NH2 A:ARG1166 4.8 79.0 1.0
CA A:CYS1258 4.8 55.4 1.0
O A:CYS1164 4.8 72.1 1.0
CD1 A:LEU1168 4.8 68.3 1.0
NH2 A:ARG1645 4.9 53.4 1.0
N A:CYS1163 5.0 64.2 1.0

Zinc binding site 2 out of 7 in 4bhw

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Zinc binding site 2 out of 7 in the Structural Basis For Autoinhibition of the Acetyltransferase Activity of P300


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structural Basis For Autoinhibition of the Acetyltransferase Activity of P300 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn2

b:74.8
occ:1.00
 SG A:CYS1272 2.3 78.6 1.0
SG A:CYS1275 2.3 82.4 1.0
CB A:CYS1250 2.4 83.2 1.0
SG A:CYS1247 2.4 83.5 1.0
SG A:CYS1250 2.8 0.6 1.0
CB A:CYS1247 3.4 80.1 1.0
CA A:CYS1250 3.4 90.8 1.0
N A:CYS1250 3.4 95.8 1.0
CB A:CYS1272 3.5 82.0 1.0
CB A:CYS1275 3.6 90.9 1.0
N A:CYS1272 4.1 76.9 1.0
N A:CYS1275 4.3 87.3 1.0
CA A:CYS1272 4.3 80.8 1.0
C A:GLU1249 4.5 96.6 1.0
CA A:CYS1275 4.6 88.8 1.0
O A:CYS1272 4.7 88.5 1.0
C A:CYS1250 4.7 90.2 1.0
C A:CYS1272 4.8 84.9 1.0
CA A:CYS1247 4.8 76.4 1.0
CB A:GLU1249 4.9 95.8 1.0
NH1 A:ARG1252 4.9 88.4 1.0
CE A:MET1254 4.9 64.1 1.0
N A:GLY1251 5.0 88.8 1.0

Zinc binding site 3 out of 7 in 4bhw

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Zinc binding site 3 out of 7 in the Structural Basis For Autoinhibition of the Acetyltransferase Activity of P300


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Structural Basis For Autoinhibition of the Acetyltransferase Activity of P300 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn3

b:0.3
occ:1.00
 SG A:CYS1201 2.2 0.1 1.0
CB A:CYS1204 2.3 0.5 1.0
CB A:CYS1201 2.4 0.8 1.0
SG A:CYS1183 2.6 0.1 1.0
SG A:CYS1177 2.9 0.2 1.0
SG A:CYS1204 2.9 0.1 1.0
N A:CYS1204 3.1 1.0 1.0
CA A:CYS1204 3.2 0.6 1.0
CA A:CYS1201 3.3 0.7 1.0
O A:CYS1201 3.3 0.7 1.0
N A:CYS1201 3.6 1.0 1.0
C A:CYS1201 3.6 0.9 1.0
CB A:CYS1183 4.2 0.5 1.0
C A:LYS1203 4.3 1.0 1.0
CB A:CYS1177 4.3 0.9 1.0
C A:CYS1204 4.4 0.6 1.0
N A:LYS1203 4.6 1.0 1.0
CB A:LYS1203 4.7 0.6 1.0
CA A:LYS1203 4.7 0.1 1.0
N A:PHE1205 4.7 0.0 1.0
N A:GLU1202 4.8 0.9 1.0
C A:PHE1200 4.8 97.6 1.0

Zinc binding site 4 out of 7 in 4bhw

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Zinc binding site 4 out of 7 in the Structural Basis For Autoinhibition of the Acetyltransferase Activity of P300


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Structural Basis For Autoinhibition of the Acetyltransferase Activity of P300 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn4

b:68.5
occ:1.00
 NE2 A:HIS1315 2.0 47.4 1.0
NE2 B:HIS1315 2.0 62.9 1.0
SG B:CYS1408 2.2 79.7 1.0
SG A:CYS1408 2.4 74.1 1.0
CD2 B:HIS1315 2.6 64.6 1.0
CD2 A:HIS1315 2.8 48.4 1.0
CB A:CYS1408 3.0 38.0 1.0
CE1 A:HIS1315 3.1 54.7 1.0
CE1 B:HIS1315 3.2 71.8 1.0
CB B:CYS1408 3.5 48.7 1.0
CG B:HIS1315 3.9 67.1 1.0
CG A:HIS1315 4.0 53.5 1.0
ND1 A:HIS1315 4.1 55.4 1.0
ND1 B:HIS1315 4.1 72.3 1.0
CA A:CYS1408 4.5 36.7 1.0
CA B:CYS1408 4.8 49.0 1.0
O A:HOH2028 4.9 37.1 1.0

Zinc binding site 5 out of 7 in 4bhw

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Zinc binding site 5 out of 7 in the Structural Basis For Autoinhibition of the Acetyltransferase Activity of P300


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Structural Basis For Autoinhibition of the Acetyltransferase Activity of P300 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1

b:70.4
occ:1.00
 ND1 B:HIS1255 2.2 72.0 1.0
SG B:CYS1163 2.4 70.2 1.0
SG B:CYS1258 2.4 67.6 1.0
SG B:CYS1164 2.5 77.4 1.0
CG B:HIS1255 3.1 72.7 1.0
CE1 B:HIS1255 3.2 73.4 1.0
CB B:HIS1255 3.3 71.1 1.0
CB B:CYS1164 3.4 66.3 1.0
CB B:CYS1258 3.6 67.4 1.0
CB B:CYS1163 3.6 74.4 1.0
N B:CYS1164 3.7 70.7 1.0
CA B:CYS1164 4.0 70.1 1.0
C B:CYS1163 4.2 73.1 1.0
CD2 B:HIS1255 4.2 72.4 1.0
NE2 B:HIS1255 4.3 74.6 1.0
N B:HIS1255 4.3 76.4 1.0
C B:CYS1164 4.4 74.3 1.0
CA B:HIS1255 4.4 73.7 1.0
O B:CYS1164 4.4 79.0 1.0
CA B:CYS1163 4.5 76.3 1.0
NH2 B:ARG1166 4.5 83.2 1.0
CD1 B:LEU1168 4.6 66.4 1.0
NH2 B:ARG1645 4.6 62.5 1.0
O B:CYS1163 4.8 73.6 1.0
CA B:CYS1258 4.9 66.7 1.0
CH2 B:TRP1115 5.0 78.1 1.0

Zinc binding site 6 out of 7 in 4bhw

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Zinc binding site 6 out of 7 in the Structural Basis For Autoinhibition of the Acetyltransferase Activity of P300


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Structural Basis For Autoinhibition of the Acetyltransferase Activity of P300 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn2

b:0.4
occ:1.00
 SG B:CYS1272 2.2 0.0 1.0
SG B:CYS1250 2.5 0.3 1.0
SG B:CYS1275 2.5 0.1 1.0
SG B:CYS1247 2.7 0.4 1.0
CB B:CYS1250 2.8 0.7 1.0
CB B:CYS1272 3.2 0.7 1.0
CB B:CYS1247 3.5 0.9 1.0
CB B:CYS1275 3.6 0.7 1.0
N B:CYS1250 3.8 0.7 1.0
CA B:CYS1250 3.9 0.8 1.0
N B:CYS1272 4.1 0.5 1.0
CA B:CYS1272 4.2 0.7 1.0
N B:CYS1275 4.3 0.2 1.0
CA B:CYS1275 4.5 0.8 1.0
NE B:ARG1252 4.7 0.0 1.0
C B:CYS1250 4.8 0.1 1.0
N B:GLY1251 4.8 0.3 1.0
C B:CYS1272 4.9 0.4 1.0
C B:GLU1249 5.0 0.1 1.0
CA B:CYS1247 5.0 0.7 1.0
CB B:GLU1249 5.0 0.7 1.0
O B:CYS1272 5.0 0.3 1.0

Zinc binding site 7 out of 7 in 4bhw

Go back to Zinc Binding Sites List in 4bhw
Zinc binding site 7 out of 7 in the Structural Basis For Autoinhibition of the Acetyltransferase Activity of P300


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Structural Basis For Autoinhibition of the Acetyltransferase Activity of P300 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn3

b:0.1
occ:1.00
 SG B:CYS1201 2.2 0.1 1.0
CB B:CYS1201 2.3 0.6 1.0
SG B:CYS1183 2.4 0.2 1.0
CB B:CYS1204 2.4 0.8 1.0
SG B:CYS1177 2.8 0.8 1.0
SG B:CYS1204 2.8 0.8 1.0
N B:CYS1204 3.4 0.3 1.0
CA B:CYS1204 3.4 0.9 1.0
CA B:CYS1201 3.5 0.3 1.0
N B:CYS1201 3.7 0.7 1.0
C B:CYS1201 3.9 0.6 1.0
O B:CYS1201 4.0 0.9 1.0
CB B:CYS1183 4.1 1.0 1.0
CB B:CYS1177 4.3 0.3 1.0
C B:LYS1203 4.6 0.7 1.0
C B:CYS1204 4.7 0.6 1.0
N B:LYS1203 4.8 0.3 1.0
N B:GLU1202 4.8 0.7 1.0
C B:PHE1200 4.9 1.0 1.0
N B:PHE1205 5.0 0.5 1.0

Reference:

M.Delvecchio, J.Gaucher, C.Aguilar-Gurrieri, E.Ortega, D.Panne. Structure of the P300 Catalytic Core and Implications For Chromatin Targeting and Hat Regulation Nat.Struct.Mol.Biol. V. 20 1040 2013.
ISSN: ISSN 1545-9993
PubMed: 23934153
DOI: 10.1038/NSMB.2642
Page generated: Sat Oct 26 19:47:31 2024

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