Structure of PDB 4psx Chain D

Receptor sequence
>4psxD (length=313) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
KPETWTSSANEALRVSIVGENAVQFSPLFTYPIYGDSEKIYGYKDLIIHL
AFDSVTFKPYVNVKYSAKLGDDNIVDVEKKLLSFLPKDDVIVRDEAKWVD
CFAEERKTHNLSDVFEKVSEYSLNGEEFVVYKSSLVDDFARRMHRRVQIF
SLLFIEAANYIDETDPSWQIYWLLNKKTKELIGFVTTYKYWHYLGAKSFD
EDIDKKFRAKISQFLIFPPYQNKGHGSCLYEAIIQSWLEDKSITEITVED
PNEAFDDLRDRNDIQRLRKLGYDAVFQKHSDLSDEFLESSRKSLKLEERQ
FNRLVEMLLLLNN
3D structure
PDB4psx Hat2p recognizes the histone H3 tail to specify the acetylation of the newly synthesized H3/H4 heterodimer by the Hat1p/Hat2p complex
ChainD
Resolution2.509 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) F220 E255
Catalytic site (residue number reindexed from 1) F214 E249
Enzyme Commision number 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 D I161 F220 L221 I222 Q227 N228 G230 G232 S233 N258 L264 R267 I155 F214 L215 I216 Q221 N222 G224 G226 S227 N252 L258 R261
Gene Ontology
Molecular Function
GO:0004402 histone acetyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
GO:0042393 histone binding
Biological Process
GO:0006325 chromatin organization
GO:0031509 subtelomeric heterochromatin formation
Cellular Component
GO:0005634 nucleus

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4psx, PDBe:4psx, PDBj:4psx
PDBsum4psx
PubMed24835250
UniProtQ12341|HAT1_YEAST Histone acetyltransferase type B catalytic subunit (Gene Name=HAT1)

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