Structure of PDB 6pgu Chain A

Receptor sequence
>6pguA (length=313) Species: 9606 (Homo sapiens) [Search protein sequence]
SKFSAKRLPSTRLGTFLENRVNDFLRRQNHPESGEVTVRVVHASDKTVEV
KPGMKARFVDSGEMAESFPYRTKALFAFEEIDGVDLCFFGMHVQEYGSDC
PPPNQRRVYISYLDSVHFFRPKCLRTAVYHEILIGYLEYVKKLGYTTGHI
WACPPSEGDDYIFHCHPPDQKIPKPKRLQEWFKKMLDKAVSERIVHDYKD
IFKQATEDRLTSAKELPYFEGDFWPNVLEESIQKLYATMEKHKEVFFVIR
LIAGPAANSLPPIVDPDPLIPCDLMDGRDAFLTLARDKHLEFSSLRRAQW
STMCMLVELHTQS
3D structure
PDB6pgu Make the right measurement: Discovery of an allosteric inhibition site for p300-HAT.
ChainA
Resolution1.72 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 2.3.1.-
2.3.1.48: histone acetyltransferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 COA A L1398 D1399 S1400 R1410 T1411 Y1414 W1436 P1440 Y1446 K1456 I1457 P1458 R1462 W1466 L113 D114 S115 R125 T126 Y129 W151 P155 Y161 K171 I172 P173 R177 W181 BindingDB: IC50=45940nM
BS02 OK7 A Y1394 H1434 I1435 I1486 P1502 D1507 F1595 F1596 Y109 H149 I150 I201 P217 D222 F246 F247 MOAD: ic50=20uM
Gene Ontology
Molecular Function
GO:0004402 histone acetyltransferase activity
Biological Process
GO:0006355 regulation of DNA-templated transcription

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6pgu, PDBe:6pgu, PDBj:6pgu
PDBsum6pgu
PubMed31649965
UniProtQ09472|EP300_HUMAN Histone acetyltransferase p300 (Gene Name=EP300)

[Back to BioLiP]