Structure of PDB 7vi0 Chain B

Receptor sequence
>7vi0B (length=433) Species: 9606 (Homo sapiens) [Search protein sequence]
YCCGRKLEFSPQTLCCYGKQLCTIPRDATYYSYQNRYHFCEKCFNEIQGE
SVSLGQTTINKEQFSKRKNDTLDPELFVECTECGRKMHQICVLHHEIIWP
AGFVCDGCLKKSARTRKENKFSAKRLPSTRLGTFLENRVNDFLRRQNHPE
SGEVTVRVVHASDKTVEVKPGMKARFVDSGEMAESFPYRTKALFAFEEID
GVDLCFFGMHVQEYGSDCPPPNQRRVYISYLDSVHFFRPKCLRTAVYHEI
LIGYLEYVKKLGYTTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWF
KKMLDKAVSERIVHDYKDIFKQATEDRLTSAKELPYFEGDFWPNVLEESI
KESGGSGSQKLYATMEKHKEVFFVIRLIASLPPIVDPDPLIPCDLMDGRD
AFLTLARDKHLEFSSLRRAQWSTMCMLVELHTQ
3D structure
PDB7vi0 Discovery of EP300/CBP histone acetyltransferase inhibitors through scaffold hopping of 1,4-oxazepane ring.
ChainB
Resolution2.1 Å
3D
structure
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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 ZN B C1164 H1255 C1258 C3 H88 C91
BS02 ZN B C1247 C1272 C1275 C80 C105 C108
BS03 ZN B C1177 C1183 C1201 C16 C22 C40
BS04 6YI B D1399 S1400 Y1414 P1440 D1444 H1451 Q1455 I1457 P1458 L1463 W1466 D232 S233 Y247 P273 D277 H284 Q288 I290 P291 L296 W299
Gene Ontology
Molecular Function
GO:0004402 histone acetyltransferase activity
Biological Process
GO:0006355 regulation of DNA-templated transcription

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Molecular Function
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Biological Process
External links
PDB RCSB:7vi0, PDBe:7vi0, PDBj:7vi0
PDBsum7vi0
PubMed35413416
UniProtQ09472|EP300_HUMAN Histone acetyltransferase p300 (Gene Name=EP300)

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