4PZS: P300 histone acetyltransferase domain

Name: PDB 4PZS: Crystal structure of p300 histone acetyltransferase domain in complex with Acetyl-Coenzyme A
Published: 2014-06-11
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: transferase

Crystal structure of p300 histone acetyltransferase domain in complex with Acetyl-Coenzyme A. Determined by X-ray diffraction at 1.94 Å resolution. Released 11 Jun 2014.

Method: X-ray diffraction
Resolution: 1.94 Å
Organism: Homo sapiens
Chains: 1
Atoms: 3,055
Mol. weight: 44.59 kDa
Ligands: ACO
Released: 11 Jun 2014

Explore 4PZS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4PZS contains 21 α-helices and 8 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 21 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	1294-1295	2
α-helix	1297-1313	17
β-strand	1321-1334	14	1
α-helix	1335-1336	2
α-helix	1337-1339	3
α-helix	1340-1344	5
β-strand	1352-1366	15	1
β-strand	1369-1381	13	1
α-helix	1386	1
β-strand	1392-1400	9	1
α-helix	1407-1409	3
α-helix	1410-1428	19
β-strand	1432-1436	5	1
α-helix	1439-1441	3
α-helix	1456-1459	4
α-helix	1460-1476	17
β-strand	1482-1485	4	1
α-helix	1486-1492	7
α-helix	1498-1500	3
α-helix	1508-1531	24
α-helix	1580-1590	11
α-helix	1592-1594	3
β-strand	1595-1599	5	1
α-helix	1609-1612	4
α-helix	1617-1618	2
β-strand	1619	1	1
α-helix	1622-1624	3
α-helix	1628-1637	10
α-helix	1644-1662	19

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Histone acetyltransferase p300	A	protein	378	Homo sapiens	Q09472 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4PZS_1 Histone acetyltransferase p300 (chains A)
KFSAKRLPSTRLGTFLENRVNDFLRRQNHPESGEVTVRVVHASDKTVEVKPGMKARFVDS
GEMAESFPYRTKALFAFEEIDGVDLCFFGMHVQEYGSDCPPPNQRRVYISYLDSVHFFRP
KCLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEW
FKKMLDKAVSERIVHDYKDIFKQATEDRLTSAKELPYFEGDFWPNVLEESIKELEQEEEE
RKREENTSNESTDVTKGDSKNAKKKNNKKTSKNKSSLSRGNKKKPGMPNVSNDLSQKLYA
TMEKHKEVFFVIRLIAGPAANSLPPIVDPDPLIPCDLMDGRDAFLTLARDKHLEFSSLRR
AQWSTMCMLVELHTQSQD

Ligands and cofactors

ID	Name	Formula	Copies
ACO	Acetyl coenzyme *a	C23 H38 N7 O17 P3 S	1

Water and common crystallization additives (DMS) are not listed.

Primary citation

Structure of the p300 Histone Acetyltransferase Bound to Acetyl-Coenzyme A and Its Analogues. Maksimoska, J., Segura-Pena, D., Cole, P.A. et al. Biochemistry (2014) 53:3415-3422. DOI 10.1021/bi500380f · PubMed

Other PDB entries of the same protein (UniProt Q09472 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5BT3 1.05 Å, Crystal structure of EP300 bromodomain in complex with SGC-CBP30 chemical probe
3T92 1.5 Å, Crystal structure of the Taz2:C/EBPepsilon-TAD chimera protein
5LPM 1.5 Å, Crystal structure of the bromodomain of human Ep300 bound to the inhibitor XDM3d
5NU5 1.6 Å, Crystal structure of the human bromodomain of EP300 bound to the inhibitor XDM-CBP
3BIY 1.7 Å, Crystal structure of p300 histone acetyltransferase domain in complex with a bisubstrate…
6PGU 1.72 Å, Crystal structure of the p300 acetyltransferase domain with allosteric inhibitor CPI-076…
6V8K 1.84 Å, Crystal structure of the p300 acetyltransferase domain with peptide-competitive…
5KJ2 1.95 Å, The novel p300/CBP inhibitor A-485 uncovers a unique mechanism of action to target AR in…
6DS6 1.95 Å, Crystal structure of p300 ZZ domain in complex with histone H3 peptide
7QGS 2.0 Å, Crystal structure of p300 CH1 domain in complex with CITIF (a CITED2-HIF-1alpha hybrid)
7UGI 2.0 Å, Bromodomain of EP300 liganded with BMS-536924
7VHZ 2.0 Å, Crystal structure of EP300 HAT domain in complex with compound 7

Browse structure collections

About this viewer

MolViewer shows 4PZS directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.